A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.
A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).
Behaviors associated with the ingesting of alcoholic beverages, including social drinking.
Alkyl compounds containing a hydroxyl group. They are classified according to relation of the carbon atom: primary alcohols, R-CH2OH; secondary alcohols, R2-CHOH; tertiary alcohols, R3-COH. (From Grant & Hackh's Chemical Dictionary, 5th ed)
A clear, colorless liquid rapidly absorbed from the gastrointestinal tract and distributed throughout the body. It has bactericidal activity and is used often as a topical disinfectant. It is widely used as a solvent and preservative in pharmaceutical preparations as well as serving as the primary ingredient in ALCOHOLIC BEVERAGES.
A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.
An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. This enzyme was formerly classified as EC 1.1.1.70.
A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)
Oxidoreductases that are specific for ALDEHYDES.
An alcohol oxidoreductase which catalyzes the oxidation of L-iditol to L-sorbose in the presence of NAD. It also acts on D-glucitol to form D-fructose. It also acts on other closely related sugar alcohols to form the corresponding sugar. EC 1.1.1.14
A colorless, flammable liquid used in the manufacture of acetic acid, perfumes, and flavors. It is also an intermediate in the metabolism of alcohol. It has a general narcotic action and also causes irritation of mucous membranes. Large doses may cause death from respiratory paralysis.
Large, hoofed mammals of the family EQUIDAE. Horses are active day and night with most of the day spent seeking and consuming food. Feeding peaks occur in the early morning and late afternoon, and there are several daily periods of rest.
Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.
Reversibly catalyzes the oxidation of a hydroxyl group of sugar alcohols to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2. and EC 1.1.99.
An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.
An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.
Glucose-6-Phosphate Dehydrogenase (G6PD) is an enzyme that plays a critical role in the pentose phosphate pathway, catalyzing the oxidation of glucose-6-phosphate to 6-phosphoglucono-δ-lactone while reducing nicotinamide adenine dinucleotide phosphate (NADP+) to nicotinamide adenine dinucleotide phosphate hydrogen (NADPH), thereby protecting cells from oxidative damage and maintaining redox balance.
The rate dynamics in chemical or physical systems.
An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41.
Alcohols derived from the aryl radical (C6H5CH2-) and defined by C6H5CHOH. The concept includes derivatives with any substituents on the benzene ring.
Isomeric forms and derivatives of butanol (C4H9OH).
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A primary, chronic disease with genetic, psychosocial, and environmental factors influencing its development and manifestations. The disease is often progressive and fatal. It is characterized by impaired control over drinking, preoccupation with the drug alcohol, use of alcohol despite adverse consequences, and distortions in thinking, most notably denial. Each of these symptoms may be continuous or periodic. (Morse & Flavin for the Joint Commission of the National Council on Alcoholism and Drug Dependence and the American Society of Addiction Medicine to Study the Definition and Criteria for the Diagnosis of Alcoholism: in JAMA 1992;268:1012-4)
Reversibly catalyze the oxidation of a hydroxyl group of carbohydrates to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2.; and 1.1.99.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
A colorless liquid with a sharp burning taste and slight odor. It is used as a local anesthetic and to reduce pain associated with LIDOCAINE injection. Also, it is used in the manufacture of other benzyl compounds, as a pharmaceutic aid, and in perfumery and flavoring.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
A glucose dehydrogenase that catalyzes the oxidation of beta-D-glucose to form D-glucono-1,5-lactone, using NAD as well as NADP as a coenzyme.
Glycerolphosphate Dehydrogenase is an enzyme (EC 1.1.1.8) that catalyzes the reversible conversion of dihydroxyacetone phosphate to glycerol 3-phosphate, using nicotinamide adenine dinucleotide (NAD+) as an electron acceptor in the process.
A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.
A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II.
Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)
Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
A colorless liquid made by oxidation of aliphatic hydrocarbons that is used as a solvent and chemical intermediate.
Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.
Benzaldehydes are aromatic organic compounds consisting of a benzene ring connected to a formyl group (-CHO), which is the simplest and most representative compound being benzaldehyde (C6H5CHO).
Organic compounds containing a carbonyl group in the form -CHO.
D-Glucose:1-oxidoreductases. Catalyzes the oxidation of D-glucose to D-glucono-gamma-lactone and reduced acceptor. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.47; EC 1.1.1.118; EC 1.1.1.119 and EC 1.1.99.10.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
The Ketoglutarate Dehydrogenase Complex is a multi-enzyme complex involved in the citric acid cycle, catalyzing the oxidative decarboxylation of alpha-ketoglutarate to succinyl-CoA and CO2, thereby connecting the catabolism of amino acids, carbohydrates, and fats to the generation of energy in the form of ATP.
Sugar alcohol dehydrogenases that have specificity for MANNITOL. Enzymes in this category are generally classified according to their preference for a specific reducing cofactor.
Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in the presence of NAD. They are key enzymes in the oxidation of fatty acids and in mitochondrial fatty acid synthesis.
A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.
A colorless, flammable liquid used in the manufacture of FORMALDEHYDE and ACETIC ACID, in chemical synthesis, antifreeze, and as a solvent. Ingestion of methanol is toxic and may cause blindness.
Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.
An enzyme of the oxidoreductase class that catalyzes the reaction 6-phospho-D-gluconate and NADP+ to yield D-ribulose 5-phosphate, carbon dioxide, and NADPH. The reaction is a step in the pentose phosphate pathway of glucose metabolism. (From Dorland, 27th ed) EC 1.1.1.43.
A species of gram-negative bacteria of the family ACETOBACTERACEAE found in FLOWERS and FRUIT. Cells are ellipsoidal to rod-shaped and straight or slightly curved.
A flavoprotein and iron sulfur-containing oxidoreductase that catalyzes the oxidation of NADH to NAD. In eukaryotes the enzyme can be found as a component of mitochondrial electron transport complex I. Under experimental conditions the enzyme can use CYTOCHROME C GROUP as the reducing cofactor. The enzyme was formerly listed as EC 1.6.2.1.
Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.
Isomeric forms and derivatives of PROPANOL (C3H7OH).
An enzyme that catalyzes the dehydrogenation of inosine 5'-phosphate to xanthosine 5'-phosphate in the presence of NAD. EC 1.1.1.205.
Hydroxybutyrate Dehydrogenase is an enzyme involved in the metabolism of certain acids, specifically catalyzing the reversible conversion of D-3-hydroxybutyrate to acetoacetate.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Alcohol oxidoreductases with substrate specificity for LACTIC ACID.
A pyrrolo-quinoline having two adjacent keto-groups at the 4 and 5 positions and three acidic carboxyl groups. It is a coenzyme of some DEHYDROGENASES.
An acute brain syndrome which results from the excessive ingestion of ETHANOL or ALCOHOLIC BEVERAGES.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Flavoproteins that catalyze reversibly the reduction of carbon dioxide to formate. Many compounds can act as acceptors, but the only physiologically active acceptor is NAD. The enzymes are active in the fermentation of sugars and other compounds to carbon dioxide and are the key enzymes in obtaining energy when bacteria are grown on formate as the main carbon source. They have been purified from bovine blood. EC 1.2.1.2.
A very loosely defined group of drugs that tend to reduce the activity of the central nervous system. The major groups included here are ethyl alcohol, anesthetics, hypnotics and sedatives, narcotics, and tranquilizing agents (antipsychotics and antianxiety agents).
A flavoprotein oxidoreductase that has specificity for medium-chain fatty acids. It forms a complex with ELECTRON TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.
An enzyme that catalyzes the oxidation of XANTHINE in the presence of NAD+ to form URIC ACID and NADH. It acts also on a variety of other purines and aldehydes.
A metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with ANEMIA, short stature, HYPOGONADISM, impaired WOUND HEALING, and geophagia. It is known by the symbol Zn.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Catalyzes the decarboxylation of an alpha keto acid to an aldehyde and carbon dioxide. Thiamine pyrophosphate is an essential cofactor. In lower organisms, which ferment glucose to ethanol and carbon dioxide, the enzyme irreversibly decarboxylates pyruvate to acetaldehyde. EC 4.1.1.1.
A group of irregular rod-shaped bacteria that stain gram-positive and do not produce endospores.
A ketone oxidoreductase that catalyzes the overall conversion of alpha-keto acids to ACYL-CoA and CO2. The enzyme requires THIAMINE DIPHOSPHATE as a cofactor. Defects in genes that code for subunits of the enzyme are a cause of MAPLE SYRUP URINE DISEASE. The enzyme was formerly classified as EC 1.2.4.3.
A metalloflavoprotein enzyme involved the metabolism of VITAMIN A, this enzyme catalyzes the oxidation of RETINAL to RETINOIC ACID, using both NAD+ and FAD coenzymes. It also acts on both the 11-trans- and 13-cis-forms of RETINAL.
Anaerobic degradation of GLUCOSE or other organic nutrients to gain energy in the form of ATP. End products vary depending on organisms, substrates, and enzymatic pathways. Common fermentation products include ETHANOL and LACTIC ACID.
An umbrella term used to describe a pattern of disabilities and abnormalities that result from fetal exposure to ETHANOL during pregnancy. It encompasses a phenotypic range that can vary greatly between individuals, but reliably includes one or more of the following: characteristic facial dysmorphism, FETAL GROWTH RETARDATION, central nervous system abnormalities, cognitive and/or behavioral dysfunction, BIRTH DEFECTS. The level of maternal alcohol consumption does not necessarily correlate directly with disease severity.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Drinkable liquids containing ETHANOL.
The E1 component of the multienzyme PYRUVATE DEHYDROGENASE COMPLEX. It is composed of 2 alpha subunits (pyruvate dehydrogenase E1 alpha subunit) and 2 beta subunits (pyruvate dehydrogenase E1 beta subunit).
Propane is a colorless, odorless, and chemically simple hydrocarbon (C3H8), commonly used as a fuel for heating, cooking, and engines, which exists as a gas at room temperature but can be liquefied under pressure and stored in cylinders or tanks.
Oxidoreductases that are specific for KETONES.
Hydroxysteroid dehydrogenases that catalyzes the reversible conversion of CORTISOL to the inactive metabolite CORTISONE. Enzymes in this class can utilize either NAD or NADP as cofactors.
Electrophoresis in which a starch gel (a mixture of amylose and amylopectin) is used as the diffusion medium.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
The most abundant natural aromatic organic polymer found in all vascular plants. Lignin together with cellulose and hemicellulose are the major cell wall components of the fibers of all wood and grass species. Lignin is composed of coniferyl, p-coumaryl, and sinapyl alcohols in varying ratios in different plant species. (From Merck Index, 11th ed)
An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.
An oxidoreductase involved in pyrimidine base degradation. It catalyzes the catabolism of THYMINE; URACIL and the chemotherapeutic drug, 5-FLUOROURACIL.
Isomeric forms and derivatives of pentanol (C5H11OH).
A genus of gram-negative, rod-shaped to ellipsoidal bacteria occurring singly or in pairs and found in flowers, soil, honey bees, fruits, cider, beer, wine, and vinegar. (From Bergey's Manual of Determinative Bacteriology, 9th ed)
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
The sum of the weight of all the atoms in a molecule.
A species of fruit fly much used in genetics because of the large size of its chromosomes.
A disease-producing enzyme deficiency subject to many variants, some of which cause a deficiency of GLUCOSE-6-PHOSPHATE DEHYDROGENASE activity in erythrocytes, leading to hemolytic anemia.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
An NAD-dependent enzyme that catalyzes the reversible DEAMINATION of L-ALANINE to PYRUVATE and AMMONIA. The enzyme is needed for growth when ALANINE is the sole CARBON or NITROGEN source. It may also play a role in CELL WALL synthesis because L-ALANINE is an important constituent of the PEPTIDOGLYCAN layer.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
A low-affinity 11 beta-hydroxysteroid dehydrogenase found in a variety of tissues, most notably in LIVER; LUNG; ADIPOSE TISSUE; vascular tissue; OVARY; and the CENTRAL NERVOUS SYSTEM. The enzyme acts reversibly and can use either NAD or NADP as cofactors.
A genus of gram-negative, facultatively anaerobic, rod-shaped bacteria that is not known to be pathogenic for man, animals, or plants. Its organisms are spoilers for beers and ciders and in sweet English ciders they are the causative agents of a secondary fermentation known as "cider sickness." The species Z. mobilis is used for experiments in molecular genetic studies.
A 3-hydroxysteroid dehydrogenase which catalyzes the reversible reduction of the active androgen, DIHYDROTESTOSTERONE to 5 ALPHA-ANDROSTANE-3 ALPHA,17 BETA-DIOL. It also has activity towards other 3-alpha-hydroxysteroids and on 9-, 11- and 15- hydroxyprostaglandins. The enzyme is B-specific in reference to the orientation of reduced NAD or NADPH.
A carbamate derivative used as an alcohol deterrent. It is a relatively nontoxic substance when administered alone, but markedly alters the intermediary metabolism of alcohol. When alcohol is ingested after administration of disulfiram, blood acetaldehyde concentrations are increased, followed by flushing, systemic vasodilation, respiratory difficulties, nausea, hypotension, and other symptoms (acetaldehyde syndrome). It acts by inhibiting aldehyde dehydrogenase.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
4-carbon straight chain aliphatic hydrocarbons substituted with two hydroxyl groups. The hydroxyl groups cannot be on the same carbon atom.
Usually high-molecular-weight, straight-chain primary alcohols, but can also range from as few as 4 carbons, derived from natural fats and oils, including lauryl, stearyl, oleyl, and linoleyl alcohols. They are used in pharmaceuticals, cosmetics, detergents, plastics, and lube oils and in textile manufacture. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.
Isomeric forms and derivatives of hexanol (C6H11OH).
Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.
Steroids in which one or more hydroxy groups have been substituted for hydrogen atoms either within the ring skeleton or on any of the side chains.
Isomeric forms and derivatives of octanol (C8H17OH).
Disorders related to or resulting from abuse or mis-use of alcohol.
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
A flavoprotein oxidoreductase that has specificity for short-chain fatty acids. It forms a complex with ELECTRON-TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.
A species of gram-negative, aerobic bacteria found in soil and water. Although considered to be normally nonpathogenic, this bacterium is a causative agent of nosocomial infections, particularly in debilitated individuals.
'Ketones' are organic compounds with a specific structure, characterized by a carbonyl group (a carbon double-bonded to an oxygen atom) and two carbon atoms, formed as byproducts when the body breaks down fats for energy due to lack of glucose, often seen in diabetes and starvation states.
A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms.
The functional hereditary units of BACTERIA.
Substances interfering with the metabolism of ethyl alcohol, causing unpleasant side effects thought to discourage the drinking of alcoholic beverages. Alcohol deterrents are used in the treatment of alcoholism.
The complete absence, or (loosely) the paucity, of gaseous or dissolved elemental oxygen in a given place or environment. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
A group of enzymes that catalyze the reversible reduction-oxidation reaction of 20-hydroxysteroids, such as from a 20-ketosteroid to a 20-alpha-hydroxysteroid (EC 1.1.1.149) or to a 20-beta-hydroxysteroid (EC 1.1.1.53).
An isomer of 1-PROPANOL. It is a colorless liquid having disinfectant properties. It is used in the manufacture of acetone and its derivatives and as a solvent. Topically, it is used as an antiseptic.
A colorless liquid used as a solvent and an antiseptic. It is one of the ketone bodies produced during ketoacidosis.
Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
A genus of gram-negative bacteria of the family MORAXELLACEAE, found in soil and water and of uncertain pathogenicity.
A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
An high-affinity, NAD-dependent 11-beta-hydroxysteroid dehydrogenase that acts unidirectionally to catalyze the dehydrogenation of CORTISOL to CORTISONE. It is found predominantly in mineralocorticoid target tissues such as the KIDNEY; COLON; SWEAT GLANDS; and the PLACENTA. Absence of the enzyme leads to a fatal form of childhood hypertension termed, APPARENT MINERALOCORTICOID EXCESS SYNDROME.
Proteins prepared by recombinant DNA technology.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.
A polymer prepared from polyvinyl acetates by replacement of the acetate groups with hydroxyl groups. It is used as a pharmaceutic aid and ophthalmic lubricant as well as in the manufacture of surface coatings artificial sponges, cosmetics, and other products.
Enzymes which are immobilized on or in a variety of water-soluble or water-insoluble matrices with little or no loss of their catalytic activity. Since they can be reused continuously, immobilized enzymes have found wide application in the industrial, medical and research fields.
A flavoprotein oxidoreductase that has specificity for long-chain fatty acids. It forms a complex with ELECTRON-TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.
Derivatives of formic acids. Included under this heading are a broad variety of acid forms, salts, esters, and amides that are formed with a single carbon carboxy group.
An enzyme that catalyzes the reduction of aspartic beta-semialdehyde to homoserine, which is the branch point in biosynthesis of methionine, lysine, threonine and leucine from aspartic acid. EC 1.1.1.3.
Iodinated derivatives of acetic acid. Iodoacetates are commonly used as alkylating sulfhydryl reagents and enzyme inhibitors in biochemical research.
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
A species of gram-negative, aerobic bacteria isolated from soil and water as well as clinical specimens. Occasionally it is an opportunistic pathogen.
A mitochondrial flavoprotein, this enzyme catalyzes the oxidation of 3-methylbutanoyl-CoA to 3-methylbut-2-enoyl-CoA using FAD as a cofactor. Defects in the enzyme, is associated with isovaleric acidemia (IVA).
An NAD+ dependent enzyme that catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate to 3-carboxy-4-methyl-2-oxopentanoate. It is involved in the biosynthesis of VALINE; LEUCINE; and ISOLEUCINE.
Analogs or derivatives of mandelic acid (alpha-hydroxybenzeneacetic acid).
Azoles of two nitrogens at the 1,2 positions, next to each other, in contrast with IMIDAZOLES in which they are at the 1,3 positions.
An enzyme that catalyzes the interconversion of a ketone and hydroxy group at C-20 of cortisone and other 17,20,21-trihydroxy steroids. EC 1.1.1.53.
The relationships of groups of organisms as reflected by their genetic makeup.
'Tert-butyl alcohol' is a type of alcohol, specifically a secondary alcohol, with the chemical formula (CH3)3COH, used as a solvent and synthetic intermediate in organic chemistry and as an antifreeze in industrial applications.
(Pyruvate dehydrogenase (lipoamide))-phosphate phosphohydrolase. A mitochondrial enzyme that catalyzes the hydrolytic removal of a phosphate on a specific seryl hydroxyl group of pyruvate dehydrogenase, reactivating the enzyme complex. EC 3.1.3.43.
An octameric enzyme belonging to the superfamily of amino acid dehydrogenases. Leucine dehydrogenase catalyzes the reversible oxidative deamination of L-LEUCINE, to 4-methyl-2-oxopentanoate (2-ketoisocaproate) and AMMONIA, with the corresponding reduction of the cofactor NAD+.
An enzyme that catalyzes the oxidation of 3-phosphoglycerate to 3-phosphohydroxypyruvate. It takes part in the L-SERINE biosynthesis pathway.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.
A clear, colorless, viscous organic solvent and diluent used in pharmaceutical preparations.
Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Pyruvates, in the context of medical and biochemistry definitions, are molecules that result from the final step of glycolysis, containing a carboxylic acid group and an aldehyde group, playing a crucial role in cellular metabolism, including being converted into Acetyl-CoA to enter the Krebs cycle or lactate under anaerobic conditions.
Enzymes that catalyze the oxidation of estradiol at the 17-hydroxyl group in the presence of NAD+ or NADP+ to yield estrone and NADH or NADPH. The 17-hydroxyl group can be in the alpha- or beta-configuration. EC 1.1.1.62
The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.
Benzyl compounds are organic substances that contain a benzyl group, which is a functional structure consisting of a carbon atom attached to a phenyl ring and a methylene group (-CH2-).
Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.
An enzyme that plays a role in the PENTOSES and GLUCURONATES interconversion pathway by catalyzing the oxidation of XYLITOL to D-xylulose. This enzyme has been found to be specific for NAD+.
Proteins found in any species of bacterium.
Measurement of the intensity and quality of fluorescence.
A genus of gram-positive, anaerobic bacteria in the family Thermoanaerobacteriaceae. Cultures consist of rods interspersed with coccoid cells.
An enzyme that plays a role in the GLUTAMATE and butanoate metabolism pathways by catalyzing the oxidation of succinate semialdehyde to SUCCINATE using NAD+ as a coenzyme. Deficiency of this enzyme, causes 4-hydroxybutyricaciduria, a rare inborn error in the metabolism of the neurotransmitter 4-aminobutyric acid (GABA).
The first chemical element in the periodic table. It has the atomic symbol H, atomic number 1, and atomic weight [1.00784; 1.00811]. It exists, under normal conditions, as a colorless, odorless, tasteless, diatomic gas. Hydrogen ions are PROTONS. Besides the common H1 isotope, hydrogen exists as the stable isotope DEUTERIUM and the unstable, radioactive isotope TRITIUM.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
Phenanthrolines are a class of heterocyclic compounds containing two aromatic hydrocarbon rings fused with a third ring consisting of nitrogen atoms, which have been used in the development of various pharmaceutical and chemical research applications, including as antibacterial, antifungal, and antiviral agents, enzyme inhibitors, and chelators.
Butanes are flammable, colorless gases with a mild petroleum-like odor, consisting of either one of two isomeric forms of butane (n-butane or isobutane), used primarily as fuel, in the production of a wide range of chemicals, and as a refrigerant.
Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)
Formic acid esters are organic compounds formed by the condensation of formic acid with alcohols, featuring an alkyl or aryl group bound to the carbonyl oxygen of the formic acid molecule.
An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.
An NAD-dependent glyceraldehyde-3-phosphate dehydrogenase found in the cytosol of eucaryotes. It catalyses the dehydrogenation and phosphorylation of GLYCERALDEHYDE 3-PHOSPHATE to 3-phospho-D-glyceroyl phosphate, which is an important step in the GLYCOLYSIS pathway.
A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)
Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.
Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.
Retinol and derivatives of retinol that play an essential role in metabolic functioning of the retina, the growth of and differentiation of epithelial tissue, the growth of bone, reproduction, and the immune response. Dietary vitamin A is derived from a variety of CAROTENOIDS found in plants. It is enriched in the liver, egg yolks, and the fat component of dairy products.
A family of gram-negative bacteria usually found in soil or water and including many plant pathogens and a few animal pathogens.
A product of fermentation. It is a component of the butanediol cycle in microorganisms. In mammals it is oxidized to carbon dioxide.
A four carbon linear hydrocarbon that has a hydroxy group at position 1.
A species of gram-positive, rod-shaped LACTIC ACID bacteria that is frequently used as starter culture in SILAGE fermentation, sourdough, and lactic-acid-fermented types of beer and wine.
A five-carbon sugar alcohol derived from XYLOSE by reduction of the carbonyl group. It is as sweet as sucrose and used as a noncariogenic sweetener.
A genus of motile or nonmotile gram-positive bacteria of the family Clostridiaceae. Many species have been identified with some being pathogenic. They occur in water, soil, and in the intestinal tract of humans and lower animals.
A trace element that is a component of vitamin B12. It has the atomic symbol Co, atomic number 27, and atomic weight 58.93. It is used in nuclear weapons, alloys, and pigments. Deficiency in animals leads to anemia; its excess in humans can lead to erythrocytosis.
Monohydroxy derivatives of cyclohexanes that contain the general formula R-C6H11O. They have a camphorlike odor and are used in making soaps, insecticides, germicides, dry cleaning, and plasticizers.
Presence of warmth or heat or a temperature notably higher than an accustomed norm.
A subclass of enzymes which includes all dehydrogenases acting on carbon-carbon bonds. This enzyme group includes all the enzymes that introduce double bonds into substrates by direct dehydrogenation of carbon-carbon single bonds.
The protein components of enzyme complexes (HOLOENZYMES). An apoenzyme is the holoenzyme minus any cofactors (ENZYME COFACTORS) or prosthetic groups required for the enzymatic function.
A widely used industrial solvent.
Disorders stemming from the misuse and abuse of alcohol.
An enzyme that catalyzes the conversion of prephenate to p-hydroxyphenylpyruvate in the presence of NAD. In the enteric bacteria, this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of tyrosine. EC 1.3.1.12.
The genetic constitution of the individual, comprising the ALLELES present at each GENETIC LOCUS.
Genotypic differences observed among individuals in a population.
Acrolein is an unsaturated aldehyde (C3H4O), highly reactive, toxic and naturally occurring compound that can be found in certain foods, tobacco smoke and is produced as a result of environmental pollution or industrial processes.
Used as an electron carrier in place of the flavine enzyme of Warburg in the hexosemonophosphate system and also in the preparation of SUCCINIC DEHYDROGENASE.
A species of GRAM-POSITIVE ENDOSPORE-FORMING BACTERIA in the family BACILLACEAE, found in soil, hot springs, Arctic waters, ocean sediments, and spoiled food products.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
A genus of small, two-winged flies containing approximately 900 described species. These organisms are the most extensively studied of all genera from the standpoint of genetics and cytology.

Hsp60 is targeted to a cryptic mitochondrion-derived organelle ("crypton") in the microaerophilic protozoan parasite Entamoeba histolytica. (1/1587)

Entamoeba histolytica is a microaerophilic protozoan parasite in which neither mitochondria nor mitochondrion-derived organelles have been previously observed. Recently, a segment of an E. histolytica gene was identified that encoded a protein similar to the mitochondrial 60-kDa heat shock protein (Hsp60 or chaperonin 60), which refolds nuclear-encoded proteins after passage through organellar membranes. The possible function and localization of the amebic Hsp60 were explored here. Like Hsp60 of mitochondria, amebic Hsp60 RNA and protein were both strongly induced by incubating parasites at 42 degreesC. 5' and 3' rapid amplifications of cDNA ends were used to obtain the entire E. histolytica hsp60 coding region, which predicted a 536-amino-acid Hsp60. The E. histolytica hsp60 gene protected from heat shock Escherichia coli groEL mutants, demonstrating the chaperonin function of the amebic Hsp60. The E. histolytica Hsp60, which lacked characteristic carboxy-terminal Gly-Met repeats, had a 21-amino-acid amino-terminal, organelle-targeting presequence that was cleaved in vivo. This presequence was necessary to target Hsp60 to one (and occasionally two or three) short, cylindrical organelle(s). In contrast, amebic alcohol dehydrogenase 1 and ferredoxin, which are bacteria-like enzymes, were diffusely distributed throughout the cytosol. We suggest that the Hsp60-associated, mitochondrion-derived organelle identified here be named "crypton," as its structure was previously hidden and its function is still cryptic.  (+info)

Ciprofloxacin decreases the rate of ethanol elimination in humans. (2/1587)

BACKGROUND: Extrahepatic ethanol metabolism is postulated to take place via microbial oxidation in the colon, mediated by aerobic and facultative anaerobic bacteria. AIMS: To evaluate the role of microbial ethanol oxidation in the total elimination rate of ethanol in humans by reducing gut flora with ciprofloxacin. METHODS: Ethanol was administered intravenously at the beginning and end of a one week period to eight male volunteers. Between ethanol doses volunteers received 750 mg ciprofloxacin twice daily. RESULTS: A highly significant (p=0.001) reduction in the ethanol elimination rate (EER) was detected after ciprofloxacin medication. Mean (SEM) EER was 107.0 (5.3) and 96.9 (4.8) mg/kg/h before and after ciprofloxacin, respectively. Faecal Enterobacteriaceae and Enterococcus sp. were totally absent after medication, and faecal acetaldehyde production capacity was significantly (p<0.05) decreased from 0.91 (0.15) to 0.39 (0.08) nmol/min/mg protein. Mean faecal alcohol dehydrogenase (ADH) activity was significantly (p<0. 05) decreased after medication, but ciprofloxacin did not inhibit human hepatic ADH activity in vitro. CONCLUSIONS: Ciprofloxacin treatment decreased the ethanol elimination rate by 9.4%, with a concomitant decrease in intestinal aerobic and facultative anaerobic bacteria, faecal ADH activity, and acetaldehyde production. As ciprofloxacin has no effect on liver blood flow, hepatic ADH activity, or cytochrome CYP2E1 activity, these effects are probably caused by the reduction in intestinal flora.  (+info)

Diet, genetic susceptibility and human cancer etiology. (3/1587)

There is evidence that high penetrance hereditary genes cause a number of relatively uncommon tumors in the familial setting, whereas common cancers are influenced by multiple loci that alter susceptibility to cancer and other conditions. The latter category of genes are involved in the metabolism of carcinogens (activation, detoxification) as well as those that interact with dietary exposure. This paper will consider some of the basic principles in studying susceptibility genes and provide a few examples in which they interact with dietary components.  (+info)

Ciprofloxacin administration decreases enhanced ethanol elimination in ethanol-fed rats. (4/1587)

Many colonic aerobic bacteria possess alcohol dehydrogenase (ADH) activity and are capable of oxidizing ethanol to acetaldehyde. Accordingly, some ingested ethanol can be metabolized in the colon in vivo via the bacteriocolonic pathway for ethanol oxidation. By diminishing the amount of aerobic colonic bacteria with ciprofloxacin treatment, we recently showed that the bacteriocolonic pathway may contribute up to 9% of total ethanol elimination in naive rats. In the current study we evaluated the role of the bacteriocolonic pathway in enhanced ethanol metabolism following chronic alcohol administration by diminishing the amount of gut aerobic flora by ciprofloxacin treatment. We found that ciprofloxacin treatment totally abolished the enhancement in ethanol elimination rate (EER) caused by chronic alcohol administration and significantly diminished the amount of colonic aerobic bacteria and faecal ADH activity. However, ciprofloxacin treatment had no significant effects on the hepatic microsomal ethanol-oxidizing system, hepatic ADH activity or plasma endotoxin level. Our data suggest that the decrease in the amount of the aerobic colonic bacteria and in faecal ADH activity by ciprofloxacin is primarily responsible for the decrease in the enhanced EER in rats fed alcohol chronically. Extrahepatic ethanol metabolism by gastrointestinal bacteria may therefore contribute significantly to enhanced EER.  (+info)

Linkage disequilibrium at the ADH2 and ADH3 loci and risk of alcoholism. (5/1587)

Two of the three class I alcohol dehydrogenase (ADH) genes (ADH2 and ADH3) encode known functional variants that act on alcohol with different efficiencies. Variants at both these genes have been implicated in alcoholism in some populations because allele frequencies differ between alcoholics and controls. Specifically, controls have higher frequencies of the variants with higher Vmax (ADH2*2 and ADH3*1). In samples both of alcoholics and of controls from three Taiwanese populations (Chinese, Ami, and Atayal) we found significant pairwise disequilibrium for all comparisons of the two functional polymorphisms and a third, presumably neutral, intronic polymorphism in ADH2. The class I ADH genes all lie within 80 kb on chromosome 4; thus, variants are not inherited independently, and haplotypes must be analyzed when evaluating the risk of alcoholism. In the Taiwanese Chinese we found that, only among those chromosomes containing the ADH3*1 variant (high Vmax), the proportions of chromosomes with ADH2*1 (low Vmax) and those with ADH2*2 (high Vmax) are significantly different between alcoholics and controls (P<10-5). The proportions of chromosomes with ADH3*1 and those with ADH3*2 are not significantly different between alcoholics and controls, on a constant ADH2 background (with ADH2*1, P=.83; with ADH2*2, P=.53). Thus, the observed differences in the frequency of the functional polymorphism at ADH3, between alcoholics and controls, can be accounted for by the disequilibrium with ADH2 in this population.  (+info)

Biochemical characterization of the small heat shock protein IbpB from Escherichia coli. (6/1587)

Escherichia coli IbpB was overexpressed in a strain carrying a deletion in the chromosomal ibp operon and purified by refolding. Under our experimental conditions, IbpB exhibited pronounced size heterogeneity. Basic oligomers, roughly spherical and approximately 15 nm in diameter, interacted to form larger particles in the 100-200-nm range, which themselves associated to yield loose aggregates of micrometer size. IbpB suppressed the thermal aggregation of model proteins in a concentration-dependent manner, and its CD spectrum was consistent with a mostly beta-pleated secondary structure. Incubation at high temperatures led to a partial loss of secondary structure, the progressive exposure of tryptophan residues to the solvent, the dissociation of high molecular mass aggregates into approximately 600-kDa oligomers, and an increase in surface hydrophobicity. Structural changes were reversible between 37 and 55 degrees C, and, up to 55 degrees C, hydrophobic sites were reburied upon cooling. IbpB exhibited a biphasic unfolding trend upon guanidine hydrochloride (GdnHCl) treatment and underwent comparable conformational changes upon melting and during the first GdnHCl-induced transition. However, hydrophobicity decreased with increasing GdnHCl concentrations, suggesting that efficient exposure of structured hydrophobic sites involves denaturant-sensitive structural features. By contrast, IbpB hydrophobicity rose at high NaCl concentrations and increased further at high temperatures. Our results support a model in which temperature-driven conformational changes lead to the reversible exposure of normally shielded binding sites for nonnative proteins and suggest that both hydrophobicity and charge context may determine substrate binding to IbpB.  (+info)

Nonsense mutations in the alcohol dehydrogenase gene of Drosophila melanogaster correlate with an abnormal 3' end processing of the corresponding pre-mRNA. (7/1587)

From bacteria to mammals, mutations that generate premature termination codons have been shown to result in the reduction in the abundance of the corresponding mRNA. In mammalian cells, more often than not, the reduction happens while the RNA is still associated with the nucleus. Here, it is reported that mutations in the alcohol dehydrogenase gene (Adh) of Drosophila melanogaster that generate premature termination codons lead to reduced levels of cytoplasmic and nuclear mRNA. Unexpectedly, it has been found that the poly(A) tails of Adh mRNAs and pre-mRNAs that carry a premature termination codon are longer than in the wild-type transcript. The more 5' terminal the mutation is, the longer is the poly(A) tail of the transcript. These findings suggest that the integrity of the coding region may be required for accurate mRNA 3' end processing.  (+info)

Drosophila lebanonensis alcohol dehydrogenase: pH dependence of the kinetic coefficients. (8/1587)

The alcohol dehydrogenase (ADH) from Drosophila lebanonensis shows 82% positional identity to the alcohol dehydrogenases from Drosophila melanogaster. These insect ADHs belong to the short-chain dehydrogenase/reductase family which lack metal ions in their active site. In this family, it appears that the function of zinc in medium chain dehydrogenases has been replaced by three amino acids, Ser138, Tyr151 and Lys155. The present work on D. lebanonensis ADH has been performed in order to obtain information about reaction mechanism, and possible differences in topology and electrostatic properties in the vicinity of the catalytic residues in ADHs from various species of Drosophila. Thus the pH dependence of various kinetic coefficients has been studied. Both in the oxidation of alcohols and in the reduction of aldehydes, the reaction mechanism of D. lebanonensis ADH in the pH 6-10 region was consistent with a compulsory ordered pathway, with the coenzymes as the outer substrates. Over the entire pH region, the rate limiting step for the oxidation of secondary alcohols such as propan-2-ol was the release of the coenzyme product from the enzyme-NADH complex. In the oxidation of ethanol at least two steps were rate limiting, the hydride transfer step and the dissociation of NADH from the binary enzyme-NADH product complex. In the reduction of acetaldehyde, the rate limiting step was the dissociation of NAD+ from the binary enzyme-NAD+ product complex. The pH dependences of the kon velocity curves for the two coenzymes were the opposite of each other, i.e. kon increased for NAD+ and decreased for NADH with increasing pH. The two curves appeared complex and the kon velocity for the two coenzymes seemed to be regulated by several groups in the free enzyme. The kon velocity for ethanol and the ethanol competitive inhibitor pyrazole increased with pH and was regulated through the ionization of a single group in the binary enzyme-NAD+ complex, with a pKa value of 7.1. The kon velocity for acetaldehyde was pH independent and showed that in the enzyme-NADH complex, the pKa value of the catalytic residue must be above 10. The koff velocity of NAD+ appeared to be partly regulated by the catalytic residue, and protonation resulted in an increased dissociation rate. The koff velocity for NADH and the hydride transfer step was pH independent. In D. lebanonensis ADH, the pKa value of the catalytic residue was 0.5 pH units lower than in the ADHS alleloenzyme from D. melanogaster. Thus it can be concluded that while most of the topology of the active site is mainly conserved in these two distantly related enzymes, the microenvironment and electrostatic properties around the catalytic residues differ.  (+info)

Alcohol dehydrogenase (ADH) is a group of enzymes responsible for catalyzing the oxidation of alcohols to aldehydes or ketones, and reducing equivalents such as NAD+ to NADH. In humans, ADH plays a crucial role in the metabolism of ethanol, converting it into acetaldehyde, which is then further metabolized by aldehyde dehydrogenase (ALDH) into acetate. This process helps to detoxify and eliminate ethanol from the body. Additionally, ADH enzymes are also involved in the metabolism of other alcohols, such as methanol and ethylene glycol, which can be toxic if allowed to accumulate in the body.

Alcohol oxidoreductases are a class of enzymes that catalyze the oxidation of alcohols to aldehydes or ketones, while reducing nicotinamide adenine dinucleotide (NAD+) to NADH. These enzymes play an important role in the metabolism of alcohols and other organic compounds in living organisms.

The most well-known example of an alcohol oxidoreductase is alcohol dehydrogenase (ADH), which is responsible for the oxidation of ethanol to acetaldehyde in the liver during the metabolism of alcoholic beverages. Other examples include aldehyde dehydrogenases (ALDH) and sorbitol dehydrogenase (SDH).

These enzymes are important targets for the development of drugs used to treat alcohol use disorder, as inhibiting their activity can help to reduce the rate of ethanol metabolism and the severity of its effects on the body.

'Alcohol drinking' refers to the consumption of alcoholic beverages, which contain ethanol (ethyl alcohol) as the active ingredient. Ethanol is a central nervous system depressant that can cause euphoria, disinhibition, and sedation when consumed in small to moderate amounts. However, excessive drinking can lead to alcohol intoxication, with symptoms ranging from slurred speech and impaired coordination to coma and death.

Alcohol is metabolized in the liver by enzymes such as alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). The breakdown of ethanol produces acetaldehyde, a toxic compound that can cause damage to various organs in the body. Chronic alcohol drinking can lead to a range of health problems, including liver disease, pancreatitis, cardiovascular disease, neurological disorders, and increased risk of cancer.

Moderate drinking is generally defined as up to one drink per day for women and up to two drinks per day for men, where a standard drink contains about 14 grams (0.6 ounces) of pure alcohol. However, it's important to note that there are no safe levels of alcohol consumption, and any level of drinking carries some risk to health.

In chemistry, an alcohol is a broad term that refers to any organic compound characterized by the presence of a hydroxyl (-OH) functional group attached to a carbon atom. This means that alcohols are essentially hydrocarbons with a hydroxyl group. The simplest alcohol is methanol (CH3OH), and ethanol (C2H5OH), also known as ethyl alcohol, is the type of alcohol found in alcoholic beverages.

In the context of medical definitions, alcohol primarily refers to ethanol, which has significant effects on the human body when consumed. Ethanol can act as a central nervous system depressant, leading to various physiological and psychological changes depending on the dose and frequency of consumption. Excessive or prolonged use of ethanol can result in various health issues, including addiction, liver disease, neurological damage, and increased risk of injuries due to impaired judgment and motor skills.

It is important to note that there are other types of alcohols (e.g., methanol, isopropyl alcohol) with different chemical structures and properties, but they are not typically consumed by humans and can be toxic or even lethal in high concentrations.

Ethanol is the medical term for pure alcohol, which is a colorless, clear, volatile, flammable liquid with a characteristic odor and burning taste. It is the type of alcohol that is found in alcoholic beverages and is produced by the fermentation of sugars by yeasts.

In the medical field, ethanol is used as an antiseptic and disinfectant, and it is also used as a solvent for various medicinal preparations. It has central nervous system depressant properties and is sometimes used as a sedative or to induce sleep. However, excessive consumption of ethanol can lead to alcohol intoxication, which can cause a range of negative health effects, including impaired judgment, coordination, and memory, as well as an increased risk of accidents, injuries, and chronic diseases such as liver disease and addiction.

L-Lactate Dehydrogenase (LDH) is an enzyme found in various tissues within the body, including the heart, liver, kidneys, muscles, and brain. It plays a crucial role in the process of energy production, particularly during anaerobic conditions when oxygen levels are low.

In the presence of the coenzyme NADH, LDH catalyzes the conversion of pyruvate to lactate, generating NAD+ as a byproduct. Conversely, in the presence of NAD+, LDH can convert lactate back to pyruvate using NADH. This reversible reaction is essential for maintaining the balance between lactate and pyruvate levels within cells.

Elevated blood levels of LDH may indicate tissue damage or injury, as this enzyme can be released into the circulation following cellular breakdown. As a result, LDH is often used as a nonspecific biomarker for various medical conditions, such as myocardial infarction (heart attack), liver disease, muscle damage, and certain types of cancer. However, it's important to note that an isolated increase in LDH does not necessarily pinpoint the exact location or cause of tissue damage, and further diagnostic tests are usually required for confirmation.

Aldehyde dehydrogenase (ALDH) is a class of enzymes that play a crucial role in the metabolism of alcohol and other aldehydes in the body. These enzymes catalyze the oxidation of aldehydes to carboxylic acids, using nicotinamide adenine dinucleotide (NAD+) as a cofactor.

There are several isoforms of ALDH found in different tissues throughout the body, with varying substrate specificities and kinetic properties. The most well-known function of ALDH is its role in alcohol metabolism, where it converts the toxic aldehyde intermediate acetaldehyde to acetate, which can then be further metabolized or excreted.

Deficiencies in ALDH activity have been linked to a number of clinical conditions, including alcohol flush reaction, alcohol-induced liver disease, and certain types of cancer. Additionally, increased ALDH activity has been associated with chemotherapy resistance in some cancer cells.

NAD (Nicotinamide Adenine Dinucleotide) is a coenzyme found in all living cells. It plays an essential role in cellular metabolism, particularly in redox reactions, where it acts as an electron carrier. NAD exists in two forms: NAD+, which accepts electrons and becomes reduced to NADH. This pairing of NAD+/NADH is involved in many fundamental biological processes such as generating energy in the form of ATP during cellular respiration, and serving as a critical cofactor for various enzymes that regulate cellular functions like DNA repair, gene expression, and cell death.

Maintaining optimal levels of NAD+/NADH is crucial for overall health and longevity, as it declines with age and in certain disease states. Therefore, strategies to boost NAD+ levels are being actively researched for their potential therapeutic benefits in various conditions such as aging, neurodegenerative disorders, and metabolic diseases.

Aldehyde oxidoreductases are a class of enzymes that catalyze the oxidation of aldehydes to carboxylic acids using NAD+ or FAD as cofactors. They play a crucial role in the detoxification of aldehydes generated from various metabolic processes, such as lipid peroxidation and alcohol metabolism. These enzymes are widely distributed in nature and have been identified in bacteria, yeast, plants, and animals.

The oxidation reaction catalyzed by aldehyde oxidoreductases involves the transfer of electrons from the aldehyde substrate to the cofactor, resulting in the formation of a carboxylic acid and reduced NAD+ or FAD. The enzymes are classified into several families based on their sequence similarity and cofactor specificity.

One of the most well-known members of this family is alcohol dehydrogenase (ADH), which catalyzes the oxidation of alcohols to aldehydes or ketones as part of the alcohol metabolism pathway. Another important member is aldehyde dehydrogenase (ALDH), which further oxidizes the aldehydes generated by ADH to carboxylic acids, thereby preventing the accumulation of toxic aldehydes in the body.

Deficiencies in ALDH enzymes have been linked to several human diseases, including alcoholism and certain types of cancer. Therefore, understanding the structure and function of aldehyde oxidoreductases is essential for developing new therapeutic strategies to treat these conditions.

L-Iditol 2-Dehydrogenase is an enzyme that catalyzes the chemical reaction between L-iditol and NAD+ to produce L-sorbose and NADH + H+. This enzyme plays a role in the metabolism of sugars, specifically in the conversion of L-iditol to L-sorbose in various organisms, including bacteria and fungi. The reaction catalyzed by this enzyme is part of the polyol pathway, which is involved in the regulation of osmotic pressure and other cellular processes.

Acetaldehyde is a colorless, volatile, and flammable liquid with a pungent odor. It is the simplest aldehyde, with the formula CH3CHO. Acetaldehyde is an important intermediate in the metabolism of alcohol and is produced by the oxidation of ethanol by alcohol dehydrogenase. It is also a naturally occurring compound that is found in small amounts in various foods and beverages, such as fruits, vegetables, and coffee.

Acetaldehyde is a toxic substance that can cause a range of adverse health effects, including irritation of the eyes, nose, and throat, nausea, vomiting, and headaches. It has been classified as a probable human carcinogen by the International Agency for Research on Cancer (IARC). Long-term exposure to acetaldehyde has been linked to an increased risk of certain types of cancer, including cancers of the oral cavity, esophagus, and liver.

I'm sorry for any confusion, but "horses" is not a medical term. It is the common name given to the species *Equus ferus caballus*, which are large domesticated mammals used for transportation, work, and recreation. If you have any questions about horses or a related topic that you would like a medical perspective on, please let me know and I'd be happy to help!

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is an enzyme that plays a crucial role in the metabolic pathway of glycolysis. Its primary function is to convert glyceraldehyde-3-phosphate (a triose sugar phosphate) into D-glycerate 1,3-bisphosphate, while also converting nicotinamide adenine dinucleotide (NAD+) into its reduced form NADH. This reaction is essential for the production of energy in the form of adenosine triphosphate (ATP) during cellular respiration. GAPDH has also been implicated in various non-metabolic processes, including DNA replication, repair, and transcription regulation, due to its ability to interact with different proteins and nucleic acids.

Sugar alcohol dehydrogenases (SADHs) are a group of enzymes that catalyze the interconversion between sugar alcohols and sugars, which involves the gain or loss of a pair of electrons, typically in the form of NAD(P)+/NAD(P)H. These enzymes play a crucial role in the metabolism of sugar alcohols, which are commonly found in various plants and some microorganisms.

Sugar alcohols, also known as polyols, are reduced forms of sugars that contain one or more hydroxyl groups instead of aldehyde or ketone groups. Examples of sugar alcohols include sorbitol, mannitol, xylitol, and erythritol. SADHs can interconvert these sugar alcohols to their corresponding sugars through a redox reaction that involves the transfer of hydrogen atoms.

The reaction catalyzed by SADHs is typically represented as follows:

R-CH(OH)-CH2OH + NAD(P)+ ↔ R-CO-CH2OH + NAD(P)H + H+

where R represents a carbon chain, and CH(OH)-CH2OH and CO-CH2OH represent the sugar alcohol and sugar forms, respectively.

SADHs are widely distributed in nature and have been found in various organisms, including bacteria, fungi, plants, and animals. These enzymes have attracted significant interest in biotechnology due to their potential applications in the production of sugar alcohols and other value-added products. Additionally, SADHs have been studied as targets for developing novel antimicrobial agents, as inhibiting these enzymes can disrupt the metabolism of certain pathogens that rely on sugar alcohols for growth and survival.

Malate Dehydrogenase (MDH) is an enzyme that plays a crucial role in the Krebs cycle, also known as the citric acid cycle or tricarboxylic acid (TCA) cycle. It catalyzes the reversible oxidation of malate to oxaloacetate, while simultaneously reducing NAD+ to NADH. This reaction is essential for energy production in the form of ATP and NADH within the cell.

There are two main types of Malate Dehydrogenase:

1. NAD-dependent Malate Dehydrogenase (MDH1): Found primarily in the cytoplasm, this isoform plays a role in the malate-aspartate shuttle, which helps transfer reducing equivalents between the cytoplasm and mitochondria.
2. FAD-dependent Malate Dehydrogenase (MDH2): Located within the mitochondrial matrix, this isoform is involved in the Krebs cycle for energy production.

Abnormal levels of Malate Dehydrogenase enzyme can be indicative of certain medical conditions or diseases, such as myocardial infarction (heart attack), muscle damage, or various types of cancer. Therefore, MDH enzyme activity is often assessed in diagnostic tests to help identify and monitor these health issues.

Glutamate Dehydrogenase (GLDH or GDH) is a mitochondrial enzyme that plays a crucial role in the metabolism of amino acids, particularly within liver and kidney tissues. It catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate, which links amino acid metabolism with the citric acid cycle and energy production. This enzyme is significant in clinical settings as its levels in blood serum can be used as a diagnostic marker for diseases that damage liver or kidney cells, since these cells release GLDH into the bloodstream upon damage.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), also known as Glucosephosphate Dehydrogenase, is an enzyme that plays a crucial role in cellular metabolism, particularly in the glycolytic pathway. It catalyzes the conversion of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (1,3-BPG), while also converting nicotinamide adenine dinucleotide (NAD+) to its reduced form NADH. This reaction is essential for the production of energy in the form of adenosine triphosphate (ATP) during cellular respiration. GAPDH has been widely used as a housekeeping gene in molecular biology research due to its consistent expression across various tissues and cells, although recent studies have shown that its expression can vary under certain conditions.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Isocitrate Dehydrogenase (IDH) is an enzyme that catalyzes the oxidative decarboxylation of isocitrate to α-ketoglutarate in the presence of NAD+ or NADP+, producing NADH or NADPH respectively. This reaction occurs in the citric acid cycle, also known as the Krebs cycle or tricarboxylic acid (TCA) cycle, which is a crucial metabolic pathway in the cell's energy production and biosynthesis of various molecules. There are three isoforms of IDH found in humans: IDH1 located in the cytosol, IDH2 in the mitochondrial matrix, and IDH3 within the mitochondria. Mutations in IDH1 and IDH2 have been associated with several types of cancer, such as gliomas and acute myeloid leukemia (AML), leading to abnormal accumulation of 2-hydroxyglutarate, which can contribute to tumorigenesis.

Benzyl alcohol is an aromatic alcohol with the chemical formula C6H5CH2OH. It is a colorless liquid with a mild, pleasant odor and is used as a solvent and preservative in cosmetics, medications, and other products. Benzyl alcohol can also be found as a natural component of some essential oils, fruits, and teas.

Benzyl alcohol is not typically considered a "drug" or a medication, but it may have various pharmacological effects when used in certain medical contexts. For example, it has antimicrobial properties and is sometimes used as a preservative in injectable medications to prevent the growth of bacteria and fungi. It can also be used as a local anesthetic or analgesic in some topical creams and ointments.

It's important to note that benzyl alcohol can be harmful or fatal to infants and young children, especially when it is used in high concentrations or when it is introduced into the body through intravenous (IV) routes. Therefore, it should be used with caution in these populations and only under the guidance of a healthcare professional.

Butanols are a family of alcohols with four carbon atoms and a chemical formula of C4H9OH. They are commonly used as solvents, intermediates in chemical synthesis, and fuel additives. The most common butanol is n-butanol (normal butanol), which has a straight chain of four carbon atoms. Other forms include secondary butanols (such as isobutanol) and tertiary butanols (such as tert-butanol). These compounds have different physical and chemical properties due to the differences in their molecular structure, but they all share the common characteristic of being alcohols with four carbon atoms.

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Alcoholism is a chronic and often relapsing brain disorder characterized by the excessive and compulsive consumption of alcohol despite negative consequences to one's health, relationships, and daily life. It is also commonly referred to as alcohol use disorder (AUD) or alcohol dependence.

The diagnostic criteria for AUD include a pattern of alcohol use that includes problems controlling intake, continued use despite problems resulting from drinking, development of a tolerance, drinking that leads to risky behaviors or situations, and withdrawal symptoms when not drinking.

Alcoholism can cause a wide range of physical and psychological health problems, including liver disease, heart disease, neurological damage, mental health disorders, and increased risk of accidents and injuries. Treatment for alcoholism typically involves a combination of behavioral therapies, medications, and support groups to help individuals achieve and maintain sobriety.

Carbohydrate dehydrogenases are a group of enzymes that catalyze the oxidation of carbohydrates, including sugars and sugar alcohols. These enzymes play a crucial role in cellular metabolism by helping to convert these molecules into forms that can be used for energy or as building blocks for other biological compounds.

During the oxidation process, carbohydrate dehydrogenases remove hydrogen atoms from the carbohydrate substrate and transfer them to an electron acceptor, such as NAD+ or FAD. This results in the formation of a ketone or aldehyde group on the carbohydrate molecule and the reduction of the electron acceptor to NADH or FADH2.

Carbohydrate dehydrogenases are classified into several subgroups based on their substrate specificity, cofactor requirements, and other factors. Some examples include glucose dehydrogenase, galactose dehydrogenase, and sorbitol dehydrogenase.

These enzymes have important applications in various fields, including biotechnology, medicine, and industry. For example, they can be used to detect or quantify specific carbohydrates in biological samples, or to produce valuable chemical compounds through the oxidation of renewable resources such as plant-derived sugars.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Isoenzymes, also known as isoforms, are multiple forms of an enzyme that catalyze the same chemical reaction but differ in their amino acid sequence, structure, and/or kinetic properties. They are encoded by different genes or alternative splicing of the same gene. Isoenzymes can be found in various tissues and organs, and they play a crucial role in biological processes such as metabolism, detoxification, and cell signaling. Measurement of isoenzyme levels in body fluids (such as blood) can provide valuable diagnostic information for certain medical conditions, including tissue damage, inflammation, and various diseases.

Benzyl alcohol is a aromatic alcohol with the chemical formula C6H5CH2OH. It is a colorless liquid with a characteristic, mildly unpleasant odor. Benzyl alcohol is used as a solvent and as an intermediate in the production of other chemicals. In medicine, it is used as a local anesthetic and antimicrobial agent. It can be found in some personal care products, such as cosmetics, shampoos, and sunscreens, as well as in topical medications and intravenous medications.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Glucose 1-Dehydrogenase (G1DH) is an enzyme that catalyzes the oxidation of β-D-glucose into D-glucono-1,5-lactone and reduces the cofactor NAD+ into NADH. This reaction plays a role in various biological processes, including glucose sensing and detoxification of reactive carbonyl species. G1DH is found in many organisms, including humans, and has several isoforms with different properties and functions.

Glycerol-3-phosphate dehydrogenase (GPD) is an enzyme that plays a crucial role in the metabolism of glucose and lipids. It catalyzes the conversion of dihydroxyacetone phosphate (DHAP) to glycerol-3-phosphate (G3P), which is a key intermediate in the synthesis of triglycerides, phospholipids, and other glycerophospholipids.

There are two main forms of GPD: a cytoplasmic form (GPD1) and a mitochondrial form (GPD2). The cytoplasmic form is involved in the production of NADH, which is used in various metabolic processes, while the mitochondrial form is involved in the production of ATP, the main energy currency of the cell.

Deficiencies or mutations in GPD can lead to a variety of metabolic disorders, including glycerol kinase deficiency and congenital muscular dystrophy. Elevated levels of GPD have been observed in certain types of cancer, suggesting that it may play a role in tumor growth and progression.

Dihydrolipoamide dehydrogenase (DHLD) is an enzyme that plays a crucial role in several important metabolic pathways in the human body, including the citric acid cycle and the catabolism of certain amino acids. DHLD is a component of multi-enzyme complexes, such as the pyruvate dehydrogenase complex (PDC) and the alpha-ketoglutarate dehydrogenase complex (KGDC).

The primary function of DHLD is to catalyze the oxidation of dihydrolipoamide, a reduced form of lipoamide, back to its oxidized state (lipoamide) while simultaneously reducing NAD+ to NADH. This reaction is essential for the continued functioning of the PDC and KGDC, as dihydrolipoamide is a cofactor for these enzyme complexes.

Deficiencies in DHLD can lead to serious metabolic disorders, such as maple syrup urine disease (MSUD) and riboflavin-responsive multiple acyl-CoA dehydrogenase deficiency (RR-MADD). These conditions can result in neurological symptoms, developmental delays, and metabolic acidosis, among other complications. Treatment typically involves dietary modifications, supplementation with specific nutrients, and, in some cases, enzyme replacement therapy.

Succinate dehydrogenase (SDH) is an enzyme complex that plays a crucial role in the process of cellular respiration, specifically in the citric acid cycle (also known as the Krebs cycle) and the electron transport chain. It is located in the inner mitochondrial membrane of eukaryotic cells.

SDH catalyzes the oxidation of succinate to fumarate, converting it into a molecule of fadaquate in the process. During this reaction, two electrons are transferred from succinate to the FAD cofactor within the SDH enzyme complex, reducing it to FADH2. These electrons are then passed on to ubiquinone (CoQ), which is a mobile electron carrier in the electron transport chain, leading to the generation of ATP, the main energy currency of the cell.

SDH is also known as mitochondrial complex II because it is the second complex in the electron transport chain. Mutations in the genes encoding SDH subunits or associated proteins have been linked to various human diseases, including hereditary paragangliomas, pheochromocytomas, gastrointestinal stromal tumors (GISTs), and some forms of neurodegenerative disorders.

NADP (Nicotinamide Adenine Dinucleotide Phosphate) is a coenzyme that plays a crucial role as an electron carrier in various redox reactions in the human body. It exists in two forms: NADP+, which functions as an oxidizing agent and accepts electrons, and NADPH, which serves as a reducing agent and donates electrons.

NADPH is particularly important in anabolic processes, such as lipid and nucleotide synthesis, where it provides the necessary reducing equivalents to drive these reactions forward. It also plays a critical role in maintaining the cellular redox balance by participating in antioxidant defense mechanisms that neutralize harmful reactive oxygen species (ROS).

In addition, NADP is involved in various metabolic pathways, including the pentose phosphate pathway and the Calvin cycle in photosynthesis. Overall, NADP and its reduced form, NADPH, are essential molecules for maintaining proper cellular function and energy homeostasis.

Coenzymes are small organic molecules that assist enzymes in catalyzing chemical reactions within cells. They typically act as carriers of specific atoms or groups of atoms during enzymatic reactions, facilitating the conversion of substrates into products. Coenzymes often bind temporarily to enzymes at the active site, forming an enzyme-coenzyme complex.

Coenzymes are usually derived from vitamins or minerals and are essential for maintaining proper metabolic functions in the body. Examples of coenzymes include nicotinamide adenine dinucleotide (NAD+), flavin adenine dinucleotide (FAD), and coenzyme A (CoA). When a coenzyme is used up in a reaction, it must be regenerated or replaced for the enzyme to continue functioning.

In summary, coenzymes are vital organic compounds that work closely with enzymes to facilitate biochemical reactions, ensuring the smooth operation of various metabolic processes within living organisms.

Oxidation-Reduction (redox) reactions are a type of chemical reaction involving a transfer of electrons between two species. The substance that loses electrons in the reaction is oxidized, and the substance that gains electrons is reduced. Oxidation and reduction always occur together in a redox reaction, hence the term "oxidation-reduction."

In biological systems, redox reactions play a crucial role in many cellular processes, including energy production, metabolism, and signaling. The transfer of electrons in these reactions is often facilitated by specialized molecules called electron carriers, such as nicotinamide adenine dinucleotide (NAD+/NADH) and flavin adenine dinucleotide (FAD/FADH2).

The oxidation state of an element in a compound is a measure of the number of electrons that have been gained or lost relative to its neutral state. In redox reactions, the oxidation state of one or more elements changes as they gain or lose electrons. The substance that is oxidized has a higher oxidation state, while the substance that is reduced has a lower oxidation state.

Overall, oxidation-reduction reactions are fundamental to the functioning of living organisms and are involved in many important biological processes.

1-Propanol is a primary alcohol with the chemical formula CH3CH2CH2OH. It is also known as n-propanol or propan-1-ol. It is a colorless, flammable liquid that is used as a solvent and in the production of other chemicals. 1-Propanol has a wide range of applications including as a disinfectant, an intermediate in the synthesis of other chemicals, and as a component in various industrial and consumer products such as cosmetics, cleaning agents, and pharmaceuticals. It is also used as a fuel additive to increase the octane rating of gasoline.

Hydroxysteroid dehydrogenases (HSDs) are a group of enzymes that play a crucial role in steroid hormone metabolism. They catalyze the oxidation and reduction reactions of hydroxyl groups on the steroid molecule, which can lead to the activation or inactivation of steroid hormones. HSDs are involved in the conversion of various steroids, including sex steroids (e.g., androgens, estrogens) and corticosteroids (e.g., cortisol, cortisone). These enzymes can be found in different tissues throughout the body, and their activity is regulated by various factors, such as hormones, growth factors, and cytokines. Dysregulation of HSDs has been implicated in several diseases, including cancer, diabetes, and cardiovascular disease.

Benzaldehyde is an organic compound with the formula C6H5CHO. It is the simplest aromatic aldehyde, and it consists of a benzene ring attached to a formyl group. Benzaldehyde is a colorless liquid with a characteristic almond-like odor.

Benzaldehyde occurs naturally in various plants, including bitter almonds, cherries, peaches, and apricots. It is used in many industrial applications, such as in the production of perfumes, flavorings, and dyes. In addition, benzaldehyde has been used in medical research for its potential therapeutic effects, such as its anti-inflammatory and antimicrobial properties.

However, it is important to note that benzaldehyde can be toxic in high concentrations and may cause irritation to the skin, eyes, and respiratory system. Therefore, it should be handled with care and used in accordance with appropriate safety guidelines.

Aldehydes are a class of organic compounds characterized by the presence of a functional group consisting of a carbon atom bonded to a hydrogen atom and a double bonded oxygen atom, also known as a formyl or aldehyde group. The general chemical structure of an aldehyde is R-CHO, where R represents a hydrocarbon chain.

Aldehydes are important in biochemistry and medicine as they are involved in various metabolic processes and are found in many biological molecules. For example, glucose is converted to pyruvate through a series of reactions that involve aldehyde intermediates. Additionally, some aldehydes have been identified as toxicants or environmental pollutants, such as formaldehyde, which is a known carcinogen and respiratory irritant.

Formaldehyde is also commonly used in medical and laboratory settings for its disinfectant properties and as a fixative for tissue samples. However, exposure to high levels of formaldehyde can be harmful to human health, causing symptoms such as coughing, wheezing, and irritation of the eyes, nose, and throat. Therefore, appropriate safety measures must be taken when handling aldehydes in medical and laboratory settings.

Glucose dehydrogenases (GDHs) are a group of enzymes that catalyze the oxidation of glucose to generate gluconic acid or glucuronic acid. This reaction involves the transfer of electrons from glucose to an electron acceptor, most commonly nicotinamide adenine dinucleotide (NAD+) or phenazine methosulfate (PMS).

GDHs are widely distributed in nature and can be found in various organisms, including bacteria, fungi, plants, and animals. They play important roles in different biological processes, such as glucose metabolism, energy production, and detoxification of harmful substances. Based on their cofactor specificity, GDHs can be classified into two main types: NAD(P)-dependent GDHs and PQQ-dependent GDHs.

NAD(P)-dependent GDHs use NAD+ or NADP+ as a cofactor to oxidize glucose to glucono-1,5-lactone, which is then hydrolyzed to gluconic acid by an accompanying enzyme. These GDHs are involved in various metabolic pathways, such as the Entner-Doudoroff pathway and the oxidative pentose phosphate pathway.

PQQ-dependent GDHs, on the other hand, use pyrroloquinoline quinone (PQQ) as a cofactor to catalyze the oxidation of glucose to gluconic acid directly. These GDHs are typically found in bacteria and play a role in energy production and detoxification.

Overall, glucose dehydrogenases are essential enzymes that contribute to the maintenance of glucose homeostasis and energy balance in living organisms.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Oxidoreductases are a class of enzymes that catalyze oxidation-reduction reactions, which involve the transfer of electrons from one molecule (the reductant) to another (the oxidant). These enzymes play a crucial role in various biological processes, including energy production, metabolism, and detoxification.

The oxidoreductase-catalyzed reaction typically involves the donation of electrons from a reducing agent (donor) to an oxidizing agent (acceptor), often through the transfer of hydrogen atoms or hydride ions. The enzyme itself does not undergo any permanent chemical change during this process, but rather acts as a catalyst to lower the activation energy required for the reaction to occur.

Oxidoreductases are classified and named based on the type of electron donor or acceptor involved in the reaction. For example, oxidoreductases that act on the CH-OH group of donors are called dehydrogenases, while those that act on the aldehyde or ketone groups are called oxidases. Other examples include reductases, peroxidases, and catalases.

Understanding the function and regulation of oxidoreductases is important for understanding various physiological processes and developing therapeutic strategies for diseases associated with impaired redox homeostasis, such as cancer, neurodegenerative disorders, and cardiovascular disease.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

The Ketoglutarate Dehydrogenase Complex (KGDC or α-KGDH) is a multi-enzyme complex that plays a crucial role in the Krebs cycle, also known as the citric acid cycle. It is located within the mitochondrial matrix of eukaryotic cells and functions to catalyze the oxidative decarboxylation of α-ketoglutarate into succinyl-CoA, thereby connecting the Krebs cycle to the electron transport chain for energy production.

The KGDC is composed of three distinct enzymes:

1. α-Ketoglutarate dehydrogenase (E1): This enzyme catalyzes the decarboxylation and oxidation of α-ketoglutarate to form a thioester intermediate with lipoamide, which is bound to the E2 component.
2. Dihydrolipoyl succinyltransferase (E2): This enzyme facilitates the transfer of the acetyl group from the lipoamide cofactor to CoA, forming succinyl-CoA and regenerating oxidized lipoamide.
3. Dihydrolipoyl dehydrogenase (E3): The final enzyme in the complex catalyzes the reoxidation of reduced lipoamide back to its disulfide form, using FAD as a cofactor and transferring electrons to NAD+, forming NADH.

The KGDC is subject to regulation by several mechanisms, including phosphorylation-dephosphorylation reactions that can inhibit or activate the complex, respectively. Dysfunction of this enzyme complex has been implicated in various diseases, such as neurodegenerative disorders and cancer.

Mannitol dehydrogenases are a group of enzymes that catalyze the oxidation of mannitol to mannose or the reverse reduction reaction, depending on the cofactor used. These enzymes play a crucial role in the metabolism of mannitol, a sugar alcohol found in various organisms, including bacteria, fungi, and plants.

There are two main types of mannitol dehydrogenases:

1. Mannitol-2-dehydrogenase (MT-2DH; EC 1.1.1.67): This enzyme oxidizes mannitol to fructose, using NAD+ as a cofactor. It is widely distributed in bacteria and fungi, contributing to their metabolic versatility.
2. Mannitol-1-dehydrogenase (MT-1DH; EC 1.1.1.17): This enzyme catalyzes the conversion of mannitol to mannose, using NADP+ as a cofactor. It is primarily found in plants and some bacteria, where it plays a role in osmoregulation and stress response.

In summary, mannitol dehydrogenases are enzymes that facilitate the interconversion of mannitol and its corresponding sugars (mannose or fructose) through oxidation-reduction reactions.

3-Hydroxyacyl CoA Dehydrogenases (3-HADs) are a group of enzymes that play a crucial role in the beta-oxidation of fatty acids. These enzymes catalyze the third step of the beta-oxidation process, which involves the oxidation of 3-hydroxyacyl CoA to 3-ketoacyl CoA. This reaction is an essential part of the energy-generating process that occurs in the mitochondria of cells and allows for the breakdown of fatty acids into smaller molecules, which can then be used to produce ATP, the primary source of cellular energy.

There are several different isoforms of 3-HADs, each with specific substrate preferences and tissue distributions. The most well-known isoform is the mitochondrial 3-hydroxyacyl CoA dehydrogenase (M3HD), which is involved in the oxidation of medium and long-chain fatty acids. Other isoforms include the short-chain 3-hydroxyacyl CoA dehydrogenase (SCHAD) and the long-chain 3-hydroxyacyl CoA dehydrogenase (LCHAD), which are involved in the oxidation of shorter and longer chain fatty acids, respectively.

Deficiencies in 3-HADs can lead to serious metabolic disorders, such as 3-hydroxyacyl-CoA dehydrogenase deficiency (3-HAD deficiency), which is characterized by the accumulation of toxic levels of 3-hydroxyacyl CoAs in the body. Symptoms of this disorder can include hypoglycemia, muscle weakness, cardiomyopathy, and developmental delays. Early diagnosis and treatment of 3-HAD deficiency are essential to prevent serious complications and improve outcomes for affected individuals.

17-Hydroxysteroid dehydrogenases (17-HSDs) are a group of enzymes that play a crucial role in steroid hormone biosynthesis. They are involved in the conversion of 17-ketosteroids to 17-hydroxy steroids or vice versa, by adding or removing a hydroxyl group (–OH) at the 17th carbon atom of the steroid molecule. This conversion is essential for the production of various steroid hormones, including cortisol, aldosterone, and sex hormones such as estrogen and testosterone.

There are several isoforms of 17-HSDs, each with distinct substrate specificities, tissue distributions, and functions:

1. 17-HSD type 1 (17-HSD1): This isoform primarily catalyzes the conversion of estrone (E1) to estradiol (E2), an active form of estrogen. It is mainly expressed in the ovary, breast, and adipose tissue.
2. 17-HSD type 2 (17-HSD2): This isoform catalyzes the reverse reaction, converting estradiol (E2) to estrone (E1). It is primarily expressed in the placenta, prostate, and breast tissue.
3. 17-HSD type 3 (17-HSD3): This isoform is responsible for the conversion of androstenedione to testosterone, an essential step in male sex hormone biosynthesis. It is predominantly expressed in the testis and adrenal gland.
4. 17-HSD type 4 (17-HSD4): This isoform catalyzes the conversion of dehydroepiandrosterone (DHEA) to androstenedione, an intermediate step in steroid hormone biosynthesis. It is primarily expressed in the placenta.
5. 17-HSD type 5 (17-HSD5): This isoform catalyzes the conversion of cortisone to cortisol, a critical step in glucocorticoid biosynthesis. It is predominantly expressed in the adrenal gland and liver.
6. 17-HSD type 6 (17-HSD6): This isoform catalyzes the conversion of androstenedione to testosterone, similar to 17-HSD3. However, it has a different substrate specificity and is primarily expressed in the ovary.
7. 17-HSD type 7 (17-HSD7): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the ovary.
8. 17-HSD type 8 (17-HSD8): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
9. 17-HSD type 9 (17-HSD9): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
10. 17-HSD type 10 (17-HSD10): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
11. 17-HSD type 11 (17-HSD11): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
12. 17-HSD type 12 (17-HSD12): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
13. 17-HSD type 13 (17-HSD13): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
14. 17-HSD type 14 (17-HSD14): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
15. 17-HSD type 15 (17-HSD15): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
16. 17-HSD type 16 (17-HSD16): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
17. 17-HSD type 17 (17-HSD17): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
18. 17-HSD type 18 (17-HSD18): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
19. 17-HSD type 19 (17-HSD19): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
20. 17-HSD type 20 (17-HSD20): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
21. 17-HSD type 21 (17-HSD21): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
22. 17-HSD type 22 (17-HSD22): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
23. 17-HSD type 23 (17-HSD23): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
24. 17-HSD type 24 (17-HSD24): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
25. 17-HSD type 25 (17-HSD25): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
26. 17-HSD type 26 (17-HSD26): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However

Methanol, also known as methyl alcohol or wood alcohol, is a volatile, colorless, flammable liquid with a distinctive odor similar to that of ethanol (drinking alcohol). It is used in various industrial applications such as the production of formaldehyde, acetic acid, and other chemicals. In the medical field, methanol is considered a toxic alcohol that can cause severe intoxication and metabolic disturbances when ingested or improperly consumed. Methanol poisoning can lead to neurological symptoms, blindness, and even death if not treated promptly and effectively.

3-Hydroxysteroid dehydrogenases (3-HSDs) are a group of enzymes that play a crucial role in steroid hormone biosynthesis. These enzymes catalyze the conversion of 3-beta-hydroxy steroids to 3-keto steroids, which is an essential step in the production of various steroid hormones, including progesterone, cortisol, aldosterone, and sex hormones such as testosterone and estradiol.

There are several isoforms of 3-HSDs that are expressed in different tissues and have distinct substrate specificities. For instance, 3-HSD type I is primarily found in the ovary and adrenal gland, where it catalyzes the conversion of pregnenolone to progesterone and 17-hydroxyprogesterone to 17-hydroxycortisol. On the other hand, 3-HSD type II is mainly expressed in the testes, adrenal gland, and placenta, where it catalyzes the conversion of dehydroepiandrosterone (DHEA) to androstenedione and androstenedione to testosterone.

Defects in 3-HSDs can lead to various genetic disorders that affect steroid hormone production and metabolism, resulting in a range of clinical manifestations such as adrenal insufficiency, ambiguous genitalia, and sexual development disorders.

Phosphogluconate dehydrogenase (PGD) is an enzyme that plays a crucial role in the pentose phosphate pathway, which is a metabolic pathway that supplies reducing energy to cells by converting glucose into ribose-5-phosphate and NADPH.

PGD catalyzes the third step of this pathway, in which 6-phosphogluconate is converted into ribulose-5-phosphate, with the concurrent reduction of NADP+ to NADPH. This reaction is essential for the generation of NADPH, which serves as a reducing agent in various cellular processes, including fatty acid synthesis and antioxidant defense.

Deficiencies in PGD can lead to several metabolic disorders, such as congenital nonspherocytic hemolytic anemia, which is characterized by the premature destruction of red blood cells due to a defect in the pentose phosphate pathway.

'Acetobacter' is a genus of gram-negative, aerobic, rod-shaped bacteria that are commonly found in various environments such as soil, water, and plant surfaces. They are known for their ability to oxidize alcohols to aldehydes and then to carboxylic acids, particularly the oxidation of ethanol to acetic acid. This property makes them important in the production of vinegar and other fermented foods. Some species of Acetobacter can also cause food spoilage and may be associated with certain human infections, although they are not considered primary human pathogens.

NADH dehydrogenase, also known as Complex I, is an enzyme complex in the electron transport chain located in the inner mitochondrial membrane. It catalyzes the oxidation of NADH to NAD+ and the reduction of coenzyme Q to ubiquinol, playing a crucial role in cellular respiration and energy production. The reaction involves the transfer of electrons from NADH to coenzyme Q, which contributes to the generation of a proton gradient across the membrane, ultimately leading to ATP synthesis. Defects in NADH dehydrogenase can result in various mitochondrial diseases and disorders.

Acyl-CoA dehydrogenases are a group of enzymes that play a crucial role in the body's energy production process. They are responsible for catalyzing the oxidation of various fatty acids, which are broken down into smaller molecules called acyl-CoAs in the body.

More specifically, acyl-CoA dehydrogenases facilitate the removal of electrons from the acyl-CoA molecules, which are then transferred to coenzyme Q10 and eventually to the electron transport chain. This process generates energy in the form of ATP, which is used by cells throughout the body for various functions.

There are several different types of acyl-CoA dehydrogenases, each responsible for oxidizing a specific type of acyl-CoA molecule. These include:

* Very long-chain acyl-CoA dehydrogenase (VLCAD), which oxidizes acyl-CoAs with 12 to 20 carbon atoms
* Long-chain acyl-CoA dehydrogenase (LCAD), which oxidizes acyl-CoAs with 14 to 20 carbon atoms
* Medium-chain acyl-CoA dehydrogenase (MCAD), which oxidizes acyl-CoAs with 6 to 12 carbon atoms
* Short-chain acyl-CoA dehydrogenase (SCAD), which oxidizes acyl-CoAs with 4 to 8 carbon atoms
* Isovaleryl-CoA dehydrogenase, which oxidizes isovaleryl-CoA, a specific type of branched-chain acyl-CoA molecule

Deficiencies in these enzymes can lead to various metabolic disorders, such as medium-chain acyl-CoA dehydrogenase deficiency (MCADD) or long-chain acyl-CoA dehydrogenase deficiency (LCADD), which can cause symptoms such as hypoglycemia, muscle weakness, and developmental delays.

"Propanols" is a general term that refers to a class of alcohols containing a propanol group, which is a functional group made up of a carbon atom bonded to three hydrogen atoms and a hydroxyl group (-OH). There are two primary structures for propanols: 1-propanol (n-propyl alcohol) and 2-propanol (isopropyl alcohol), which differ in the arrangement of their carbon chain.

1-Propanol, also known as n-propyl alcohol, has a linear structure with the hydroxyl group attached to one end of the carbon chain: CH3CH2CH2OH. It is a colorless liquid that is used as a solvent and in the production of other chemicals.

2-Propanol, also known as isopropyl alcohol or isopropanol, has a branched structure with the hydroxyl group attached to a branch on the second carbon atom: (CH3)2CHOH. It is a colorless, flammable liquid that is widely used as a solvent and disinfectant.

Both 1-propanol and 2-propanol have applications in various industries, including pharmaceuticals, cosmetics, and cleaning products. However, they should be handled with care due to their flammability and potential health hazards, such as irritation of the eyes, skin, and respiratory tract.

Inosine Monophosphate Dehydrogenase (IMDH or IMPDH) is an enzyme that is involved in the de novo biosynthesis of guanine nucleotides. It catalyzes the conversion of inosine monophosphate (IMP) to xanthosine monophosphate (XMP), which is the rate-limiting step in the synthesis of guanosine triphosphate (GTP).

There are two isoforms of IMPDH, type I and type II, which are encoded by separate genes. Type I IMPDH is expressed in most tissues, while type II IMPDH is primarily expressed in lymphocytes and other cells involved in the immune response. Inhibitors of IMPDH have been developed as immunosuppressive drugs to prevent rejection of transplanted organs. Defects in the gene encoding IMPDH type II have been associated with retinal degeneration and hearing loss.

Succinic semialdehyde dehydrogenase, also known as hydroxybutyrate dehydrogenase (EC 1.2.1.16), is an enzyme involved in the metabolism of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA). This enzyme catalyzes the oxidation of succinic semialdehyde to succinate, which is a key step in the GABA degradation pathway.

Deficiency in this enzyme can lead to an accumulation of succinic semialdehyde and its downstream metabolite, gamma-hydroxybutyric acid (GHB), resulting in neurological symptoms such as developmental delay, hypotonia, seizures, and movement disorders. GHB is a naturally occurring neurotransmitter and also a recreational drug known as "Grievous Bodily Harm" or "Liquid Ecstasy."

The gene that encodes for succinic semialdehyde dehydrogenase is located on chromosome 6 (6p22.3) and has been identified as ALDH5A1. Mutations in this gene can lead to succinic semialdehyde dehydrogenase deficiency, which is an autosomal recessive disorder.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

Lactate dehydrogenases (LDH) are a group of intracellular enzymes found in nearly all human cells, particularly in the heart, liver, kidneys, muscles, and brain. They play a crucial role in energy production during anaerobic metabolism, converting pyruvate to lactate while regenerating NAD+ from NADH. LDH exists as multiple isoenzymes (LDH-1 to LDH-5) in the body, each with distinct distributions and functions.

An elevated level of LDH in the blood may indicate tissue damage or injury, as these enzymes are released into the circulation following cellular destruction. Therefore, measuring LDH levels is a common diagnostic tool to assess various medical conditions, such as myocardial infarction (heart attack), liver disease, muscle damage, and some types of cancer. However, an isolated increase in LDH may not be specific enough for a definitive diagnosis, and additional tests are usually required for confirmation.

PQQ, or pyrroloquinoline quinone, is a redox cofactor that plays a role in the electron transfer chain and is involved in various redox reactions in the body. It can be found in some bacteria and plants, and there is evidence to suggest that it may also be present in human tissues. However, the exact role of PQQ as a cofactor in humans is not well understood and more research is needed to fully understand its functions and potential health benefits.

A cofactor is a non-protein chemical compound that is required for an enzyme to function. Cofactors can be inorganic ions, such as iron or magnesium, or organic molecules, like PQQ. They play a crucial role in catalyzing biochemical reactions and maintaining the structural integrity of proteins.

In summary, PQQ is a redox cofactor that may have a role in various redox reactions in the body, but its exact functions and significance in human health are still being studied.

Alcoholic intoxication, also known as alcohol poisoning, is a condition that occurs when a person consumes a large amount of alcohol in a short period of time. This can lead to an increase in the concentration of alcohol in the blood, which can affect the normal functioning of the body's organs and systems.

The symptoms of alcoholic intoxication can vary depending on the severity of the condition, but they may include:

* Confusion or disorientation
* Slurred speech
* Poor coordination
* Staggering or difficulty walking
* Vomiting
* Seizures
* Slow or irregular breathing
* Low body temperature (hypothermia)
* Pale or blue-tinged skin
* Unconsciousness or coma

Alcoholic intoxication can be a medical emergency and requires immediate treatment. If you suspect that someone has alcohol poisoning, it is important to seek medical help right away. Treatment may include supportive care, such as providing fluids and oxygen, and monitoring the person's vital signs. In severe cases, hospitalization may be necessary.

It is important to note that alcoholic intoxication can occur even at relatively low levels of alcohol consumption, especially in people who are not used to drinking or who have certain medical conditions. It is always best to drink in moderation and to be aware of the potential risks associated with alcohol consumption.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Formate dehydrogenases (FDH) are a group of enzymes that catalyze the oxidation of formic acid (formate) to carbon dioxide and hydrogen or to carbon dioxide and water, depending on the type of FDH. The reaction is as follows:

Formic acid + Coenzyme Q (or NAD+) -> Carbon dioxide + H2 (or H2O) + Reduced coenzyme Q (or NADH)

FDHs are widely distributed in nature and can be found in various organisms, including bacteria, archaea, and eukaryotes. They play a crucial role in the metabolism of many microorganisms that use formate as an electron donor for energy conservation or as a carbon source for growth. In addition to their biological significance, FDHs have attracted much interest as biocatalysts for various industrial applications, such as the production of hydrogen, reduction of CO2, and detoxification of formic acid in animal feed.

FDHs can be classified into two main types based on their cofactor specificity: NAD-dependent FDHs and quinone-dependent FDHs. NAD-dependent FDHs use nicotinamide adenine dinucleotide (NAD+) as a cofactor, while quinone-dependent FDHs use menaquinone or ubiquinone as a cofactor. Both types of FDHs have a similar reaction mechanism that involves the transfer of a hydride ion from formate to the cofactor and the release of carbon dioxide.

FDHs are composed of two subunits: a small subunit containing one or two [4Fe-4S] clusters and a large subunit containing a molybdenum cofactor (Moco) and one or two [2Fe-2S] clusters. Moco is a complex prosthetic group that consists of a pterin ring, a dithiolene group, and a molybdenum atom coordinated to three ligands: a sulfur atom from the dithiolene group, a terminal oxygen atom from a mononucleotide, and a serine residue. The molybdenum center can adopt different oxidation states (+4, +5, or +6) during the catalytic cycle, allowing for the transfer of electrons and the activation of formate.

FDHs have various applications in biotechnology and industry, such as the production of hydrogen gas, the removal of nitrate from wastewater, and the synthesis of fine chemicals. The high selectivity and efficiency of FDHs make them attractive catalysts for these processes, which require mild reaction conditions and low energy inputs. However, the stability and activity of FDHs are often limited by their sensitivity to oxygen and other inhibitors, which can affect their performance in industrial settings. Therefore, efforts have been made to improve the properties of FDHs through protein engineering, genetic modification, and immobilization techniques.

Central Nervous System (CNS) depressants are a class of drugs that slow down the activity of the CNS, leading to decreased arousal and decreased level of consciousness. They work by increasing the inhibitory effects of the neurotransmitter gamma-aminobutyric acid (GABA) in the brain, which results in sedation, relaxation, reduced anxiety, and in some cases, respiratory depression.

Examples of CNS depressants include benzodiazepines, barbiturates, non-benzodiazepine hypnotics, and certain types of pain medications such as opioids. These drugs are often used medically to treat conditions such as anxiety, insomnia, seizures, and chronic pain, but they can also be misused or abused for their sedative effects.

It is important to use CNS depressants only under the supervision of a healthcare provider, as they can have serious side effects, including addiction, tolerance, and withdrawal symptoms. Overdose of CNS depressants can lead to coma, respiratory failure, and even death.

Acyl-CoA dehydrogenase is a group of enzymes that play a crucial role in the body's energy production process. Specifically, they are involved in the breakdown of fatty acids within the cells.

More technically, acyl-CoA dehydrogenases catalyze the removal of electrons from the thiol group of acyl-CoAs, forming a trans-double bond and generating FADH2. This reaction is the first step in each cycle of fatty acid beta-oxidation, which occurs in the mitochondria of cells.

There are several different types of acyl-CoA dehydrogenases, each specific to breaking down different lengths of fatty acids. For example, very long-chain acyl-CoA dehydrogenase (VLCAD) is responsible for breaking down longer chain fatty acids, while medium-chain acyl-CoA dehydrogenase (MCAD) breaks down medium-length chains.

Deficiencies in these enzymes can lead to various metabolic disorders, such as MCAD deficiency or LC-FAOD (long-chain fatty acid oxidation disorders), which can cause symptoms like vomiting, lethargy, and muscle weakness, especially during periods of fasting or illness.

Xanthine dehydrogenase (XDH) is an enzyme involved in the metabolism of purines, which are nitrogen-containing compounds that form part of DNA and RNA. Specifically, XDH helps to break down xanthine and hypoxanthine into uric acid, a waste product that is excreted in the urine.

XDH can exist in two interconvertible forms: a dehydrogenase form (XDH) and an oxidase form (XO). In its dehydrogenase form, XDH uses NAD+ as an electron acceptor to convert xanthine into uric acid. However, when XDH is converted to its oxidase form (XO), it can use molecular oxygen as an electron acceptor instead, producing superoxide and hydrogen peroxide as byproducts. These reactive oxygen species can contribute to oxidative stress and tissue damage in the body.

Abnormal levels or activity of XDH have been implicated in various diseases, including gout, cardiovascular disease, and neurodegenerative disorders.

Zinc is an essential mineral that is vital for the functioning of over 300 enzymes and involved in various biological processes in the human body, including protein synthesis, DNA synthesis, immune function, wound healing, and cell division. It is a component of many proteins and participates in the maintenance of structural integrity and functionality of proteins. Zinc also plays a crucial role in maintaining the sense of taste and smell.

The recommended daily intake of zinc varies depending on age, sex, and life stage. Good dietary sources of zinc include red meat, poultry, seafood, beans, nuts, dairy products, and fortified cereals. Zinc deficiency can lead to various health problems, including impaired immune function, growth retardation, and developmental delays in children. On the other hand, excessive intake of zinc can also have adverse effects on health, such as nausea, vomiting, and impaired immune function.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Pyruvate decarboxylase is an enzyme that plays a crucial role in the cellular process of fermentation and gluconeogenesis. In medical and biochemical terms, pyruvate decarboxylase is defined as:

"An enzyme (EC 4.1.1.1) that catalyzes the decarboxylation of pyruvate to form acetaldehyde and carbon dioxide in the presence of thiamine pyrophosphate (TPP) as a cofactor. This reaction occurs during anaerobic metabolism, such as alcohol fermentation in yeast or bacteria, and helps to generate ATP and NADH for the cell's energy needs."

In humans, pyruvate decarboxylase is primarily found in the liver and kidneys, where it participates in gluconeogenesis – the process of generating new glucose molecules from non-carbohydrate precursors. The enzyme's activity is essential for maintaining blood glucose levels during fasting or low-carbohydrate intake.

Deficiencies in pyruvate decarboxylase can lead to metabolic disorders, such as pyruvate decarboxylase deficiency (PDC deficiency), which is characterized by lactic acidosis, developmental delays, and neurological issues. Proper diagnosis and management of these conditions often involve monitoring enzyme activity and glucose metabolism.

"Gram-Positive Asporogenous Rods, Irregular" is a medical term used to describe a specific type of bacteria. Here's the breakdown:

1. **Gram-Positive**: This refers to the bacterium's reaction to the Gram stain test, a common laboratory method used to classify bacteria based on their cell wall structure. Gram-positive bacteria retain the crystal violet stain used in this test, appearing purple under the microscope.

2. **Asporogenous**: This term indicates that the bacterium does not form endospores, which are highly resistant structures that some bacteria create in response to harsh environmental conditions. Endospores are capable of surviving extreme conditions and can germinate into vegetative cells when conditions improve. Asporogenous bacteria lack this ability.

3. **Rods**: This term describes the bacterium's shape. Rod-shaped bacteria, also known as bacilli, are longer than they are wide.

4. **Irregular**: This modifier is used when the rods are not uniform in size and shape, meaning they may vary in length or width, or both.

So, a "Gram-Positive Asporogenous Rod, Irregular" is a type of bacteria that is gram-positive (stains purple with the Gram stain), does not form endospores (asporogenous), has a rod shape (bacilli), and exhibits irregularities in its size and/or shape. Examples of such bacteria might include certain species within the genera Corynebacterium, Listeria, or Rhodococcus.

Retinal dehydrogenase, also known as Aldehyde Dehydrogenase 2 (ALDH2), is an enzyme involved in the metabolism of alcohol and other aldehydes in the body. In the eye, retinal dehydrogenase plays a specific role in the conversion of retinaldehyde to retinoic acid, which is an important molecule for the maintenance and regulation of the visual cycle and overall eye health.

Retinoic acid is involved in various physiological processes such as cell differentiation, growth, and survival, and has been shown to have a protective effect against oxidative stress in the retina. Therefore, retinal dehydrogenase deficiency or dysfunction may lead to impaired visual function and increased susceptibility to eye diseases such as age-related macular degeneration and diabetic retinopathy.

Fermentation is a metabolic process in which an organism converts carbohydrates into alcohol or organic acids using enzymes. In the absence of oxygen, certain bacteria, yeasts, and fungi convert sugars into carbon dioxide, hydrogen, and various end products, such as alcohol, lactic acid, or acetic acid. This process is commonly used in food production, such as in making bread, wine, and beer, as well as in industrial applications for the production of biofuels and chemicals.

Fetal Alcohol Spectrum Disorders (FASD) is a term used to describe a range of effects that can occur in an individual whose mother drank alcohol during pregnancy. These effects may include physical, mental, and behavioral abnormalities, and can vary in severity and combination from one individual to another.

The four diagnostic categories within FASD are:

1. Fetal Alcohol Syndrome (FAS): This is the most severe form of FASD and is characterized by a specific pattern of facial features, growth deficiencies, and central nervous system dysfunction.
2. Partial Fetal Alcohol Syndrome (pFAS): This category includes individuals who have some, but not all, of the features of FAS.
3. Alcohol-Related Neurodevelopmental Disorder (ARND): This category includes individuals who have functional or cognitive impairments due to prenatal alcohol exposure, but do not meet the criteria for FAS or pFAS.
4. Alcohol-Related Birth Defects (ARBD): This category includes individuals who have physical birth defects due to prenatal alcohol exposure.

It is important to note that FASD is a completely preventable condition, and there is no known safe amount or safe time to drink alcohol during pregnancy.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Alcoholic beverages are drinks that contain ethanol (ethyl alcohol), which is produced by the fermentation of yeast, sugars, and starches. The amount of alcohol in a drink is measured in terms of "alcohol content" or "alcohol by volume" (ABV). Different types of alcoholic beverages include:

1. Beer: A fermented beverage made from grains, such as barley, wheat, or rye. The alcohol content of beer typically ranges from 3-6% ABV.
2. Wine: A fermented beverage made from grapes or other fruits. The alcohol content of wine usually falls between 10-15% ABV.
3. Spirits (or liquors): Distilled beverages with higher alcohol content, typically ranging from 40-50% ABV. Examples include vodka, whiskey, rum, gin, and tequila.
4. Fortified wines: Wines that have had a distilled spirit added to them, increasing their alcohol content. Examples include port, sherry, and madeira, which typically contain 17-20% ABV.
5. Malt beverages: Fermented beverages made from malted barley or other grains, with additional flavorings or sweeteners. These can range in alcohol content from around 4-8% ABV.

It is important to note that excessive consumption of alcoholic beverages can lead to various health issues, including addiction, liver disease, and an increased risk of accidents and injuries. Moderate drinking is generally defined as up to one drink per day for women and up to two drinks per day for men, although individual tolerance and sensitivity to alcohol may vary.

I'm sorry for any confusion, but "Propane" is not a medical term. It is a chemical compound commonly used as a fuel for heating, cooking, and engines. Propane is a gas at room temperature and pressure, but it can be liquefied under moderate pressure and stored in cylinders or tanks.

If you have any questions about a medical term or concept, I'd be happy to try to help answer those for you!

Ketone oxidoreductases are a group of enzymes that catalyze the conversion of ketones to corresponding alcohols or vice versa, through the process of reduction or oxidation. These enzymes play an essential role in various metabolic pathways and biochemical reactions within living organisms.

In the context of medical research and diagnostics, ketone oxidoreductases have gained attention for their potential applications in the development of biosensors to detect and monitor blood ketone levels, particularly in patients with diabetes. Elevated levels of ketones in the blood (known as ketonemia) can indicate a serious complication called diabetic ketoacidosis, which requires prompt medical attention.

One example of a ketone oxidoreductase is the enzyme known as d-beta-hydroxybutyrate dehydrogenase (d-BDH), which catalyzes the conversion of d-beta-hydroxybutyrate to acetoacetate. This reaction is part of the metabolic pathway that breaks down fatty acids for energy production, and it becomes particularly important during periods of low carbohydrate availability or insulin deficiency, as seen in diabetes.

Understanding the function and regulation of ketone oxidoreductases can provide valuable insights into the pathophysiology of metabolic disorders like diabetes and contribute to the development of novel therapeutic strategies for their management.

11-Beta-Hydroxysteroid dehydrogenases (11-β-HSDs) are a group of enzymes that play a crucial role in the metabolism of steroid hormones, particularly cortisol and cortisone, which belong to the class of glucocorticoids. These enzymes exist in two isoforms: 11-β-HSD1 and 11-β-HSD2.

1. 11-β-HSD1: This isoform is primarily located within the liver, adipose tissue, and various other peripheral tissues. It functions as a NADPH-dependent reductase, converting inactive cortisone to its active form, cortisol. This enzyme helps regulate glucocorticoid action in peripheral tissues, influencing glucose and lipid metabolism, insulin sensitivity, and inflammation.
2. 11-β-HSD2: This isoform is predominantly found in mineralocorticoid target tissues such as the kidneys, colon, and salivary glands. It functions as a NAD+-dependent dehydrogenase, converting active cortisol to its inactive form, cortisone. By doing so, it protects the mineralocorticoid receptor from being overstimulated by cortisol, ensuring aldosterone specifically binds and activates this receptor to maintain proper electrolyte and fluid balance.

Dysregulation of 11-β-HSDs has been implicated in several disease states, including metabolic syndrome, type 2 diabetes, hypertension, and psychiatric disorders. Therefore, understanding the function and regulation of these enzymes is essential for developing novel therapeutic strategies to treat related conditions.

Electrophoresis, starch gel is a type of electrophoretic technique used in laboratory settings for the separation and analysis of large biomolecules such as DNA, RNA, and proteins. In this method, a gel made from cooked starch is used as the supporting matrix for the molecules being separated.

The sample containing the mixture of biomolecules is loaded onto the gel and an electric field is applied, causing the negatively charged molecules to migrate towards the positive electrode. The starch gel acts as a molecular sieve, with smaller molecules moving more quickly through the gel than larger ones. This results in the separation of the mixture into individual components based on their size and charge.

Once the separation is complete, the gel can be stained to visualize the separated bands. Different staining techniques are used depending on the type of biomolecule being analyzed. For example, proteins can be stained with dyes such as Coomassie Brilliant Blue or silver nitrate, while nucleic acids can be stained with dyes such as ethidium bromide.

Starch gel electrophoresis is a relatively simple and inexpensive technique that has been widely used in molecular biology research and diagnostic applications. However, it has largely been replaced by other electrophoretic techniques, such as polyacrylamide gel electrophoresis (PAGE), which offer higher resolution and can be automated for high-throughput analysis.

Catalysis is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst, which remains unchanged at the end of the reaction. A catalyst lowers the activation energy required for the reaction to occur, thereby allowing the reaction to proceed more quickly and efficiently. This can be particularly important in biological systems, where enzymes act as catalysts to speed up metabolic reactions that are essential for life.

I'm sorry for any confusion, but "Lignin" is not a medical term. It is a term used in the field of biology and chemistry, particularly in botany and wood science. Lignin is a complex organic polymer that binds cellulose fibers together, providing strength and rigidity to the cell walls of plants. It is a major component of wood and bark.

If you have any medical terms you would like defined or any other questions, please let me know!

Uridine Diphosphate (UDP) Glucose Dehydrogenase is an enzyme that plays a role in carbohydrate metabolism. Its systematic name is UDP-glucose:NAD+ oxidoreductase, and it catalyzes the following chemical reaction:

UDP-glucose + NAD+ -> UDP-glucuronate + NADH + H+

This enzyme helps convert UDP-glucose into UDP-glucuronate, which is a crucial component in the biosynthesis of various substances in the body, such as glycosaminoglycans and other glyconjugates. The reaction also results in the reduction of NAD+ to NADH, which is an essential coenzyme in numerous metabolic processes.

UDP-glucose dehydrogenase is widely distributed in various tissues, including the liver, kidney, and intestine. Deficiencies or mutations in this enzyme can lead to several metabolic disorders, such as glucosuria and hypermethioninemia.

"Pentanols" is not a recognized medical term. However, in chemistry, pentanols refer to a group of alcohols containing five carbon atoms. The general formula for pentanols is C5H12O, and they have various subcategories such as primary, secondary, and tertiary pentanols, depending on the type of hydroxyl (-OH) group attachment to the carbon chain.

In a medical context, alcohols like methanol and ethanol can be toxic and cause various health issues. However, there is no specific medical relevance associated with "pentanols" as a group. If you have any further questions or need information about a specific chemical compound, please let me know!

"Gluconobacter" is a genus of gram-negative, aerobic bacteria that are capable of oxidizing various alcohols and sugars into their corresponding acids. These bacteria are often found in fruit, flowers, and sap, as well as in fermented foods and beverages. They are known for their ability to rapidly and efficiently oxidize glucose into gluconic acid, which gives them their name. Some species of Gluconobacter can also cause disease in humans, particularly in individuals with weakened immune systems. In medical contexts, Gluconobacter species may be associated with infections such as bacteremia, endocarditis, and peritonitis.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

Stereoisomerism is a type of isomerism (structural arrangement of atoms) in which molecules have the same molecular formula and sequence of bonded atoms, but differ in the three-dimensional orientation of their atoms in space. This occurs when the molecule contains asymmetric carbon atoms or other rigid structures that prevent free rotation, leading to distinct spatial arrangements of groups of atoms around a central point. Stereoisomers can have different chemical and physical properties, such as optical activity, boiling points, and reactivities, due to differences in their shape and the way they interact with other molecules.

There are two main types of stereoisomerism: enantiomers (mirror-image isomers) and diastereomers (non-mirror-image isomers). Enantiomers are pairs of stereoisomers that are mirror images of each other, but cannot be superimposed on one another. Diastereomers, on the other hand, are non-mirror-image stereoisomers that have different physical and chemical properties.

Stereoisomerism is an important concept in chemistry and biology, as it can affect the biological activity of molecules, such as drugs and natural products. For example, some enantiomers of a drug may be active, while others are inactive or even toxic. Therefore, understanding stereoisomerism is crucial for designing and synthesizing effective and safe drugs.

"Pseudomonas" is a genus of Gram-negative, rod-shaped bacteria that are widely found in soil, water, and plants. Some species of Pseudomonas can cause disease in animals and humans, with P. aeruginosa being the most clinically relevant as it's an opportunistic pathogen capable of causing various types of infections, particularly in individuals with weakened immune systems.

P. aeruginosa is known for its remarkable ability to resist many antibiotics and disinfectants, making infections caused by this bacterium difficult to treat. It can cause a range of healthcare-associated infections, such as pneumonia, bloodstream infections, urinary tract infections, and surgical site infections. In addition, it can also cause external ear infections and eye infections.

Prompt identification and appropriate antimicrobial therapy are crucial for managing Pseudomonas infections, although the increasing antibiotic resistance poses a significant challenge in treatment.

Gene expression regulation, enzymologic refers to the biochemical processes and mechanisms that control the transcription and translation of specific genes into functional proteins or enzymes. This regulation is achieved through various enzymatic activities that can either activate or repress gene expression at different levels, such as chromatin remodeling, transcription factor activation, mRNA processing, and protein degradation.

Enzymologic regulation of gene expression involves the action of specific enzymes that catalyze chemical reactions involved in these processes. For example, histone-modifying enzymes can alter the structure of chromatin to make genes more or less accessible for transcription, while RNA polymerase and its associated factors are responsible for transcribing DNA into mRNA. Additionally, various enzymes are involved in post-transcriptional modifications of mRNA, such as splicing, capping, and tailing, which can affect the stability and translation of the transcript.

Overall, the enzymologic regulation of gene expression is a complex and dynamic process that allows cells to respond to changes in their environment and maintain proper physiological function.

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

'Drosophila melanogaster' is the scientific name for a species of fruit fly that is commonly used as a model organism in various fields of biological research, including genetics, developmental biology, and evolutionary biology. Its small size, short generation time, large number of offspring, and ease of cultivation make it an ideal subject for laboratory studies. The fruit fly's genome has been fully sequenced, and many of its genes have counterparts in the human genome, which facilitates the understanding of genetic mechanisms and their role in human health and disease.

Here is a brief medical definition:

Drosophila melanogaster (droh-suh-fih-luh meh-lon-guh-ster): A species of fruit fly used extensively as a model organism in genetic, developmental, and evolutionary research. Its genome has been sequenced, revealing many genes with human counterparts, making it valuable for understanding genetic mechanisms and their role in human health and disease.

Glucose-6-Phosphate Dehydrogenase (G6PD) deficiency is a genetic disorder that affects the normal functioning of an enzyme called G6PD. This enzyme is found in red blood cells and plays a crucial role in protecting them from damage.

In people with G6PD deficiency, the enzyme's activity is reduced or absent, making their red blood cells more susceptible to damage and destruction, particularly when they are exposed to certain triggers such as certain medications, infections, or foods. This can lead to a condition called hemolysis, where the red blood cells break down prematurely, leading to anemia, jaundice, and in severe cases, kidney failure.

G6PD deficiency is typically inherited from one's parents in an X-linked recessive pattern, meaning that males are more likely to be affected than females. While there is no cure for G6PD deficiency, avoiding triggers and managing symptoms can help prevent complications.

"Saccharomyces cerevisiae" is not typically considered a medical term, but it is a scientific name used in the field of microbiology. It refers to a species of yeast that is commonly used in various industrial processes, such as baking and brewing. It's also widely used in scientific research due to its genetic tractability and eukaryotic cellular organization.

However, it does have some relevance to medical fields like medicine and nutrition. For example, certain strains of S. cerevisiae are used as probiotics, which can provide health benefits when consumed. They may help support gut health, enhance the immune system, and even assist in the digestion of certain nutrients.

In summary, "Saccharomyces cerevisiae" is a species of yeast with various industrial and potential medical applications.

Enzyme stability refers to the ability of an enzyme to maintain its structure and function under various environmental conditions, such as temperature, pH, and the presence of denaturants or inhibitors. A stable enzyme retains its activity and conformation over time and across a range of conditions, making it more suitable for industrial and therapeutic applications.

Enzymes can be stabilized through various methods, including chemical modification, immobilization, and protein engineering. Understanding the factors that affect enzyme stability is crucial for optimizing their use in biotechnology, medicine, and research.

Alanine Dehydrogenase (ADH) is an enzyme that catalyzes the reversible conversion between alanine and pyruvate with the reduction of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide hydride (NADH). This reaction plays a role in the metabolism of amino acids, particularly in the catabolism of alanine.

In humans, there are multiple isoforms of ADH that are expressed in different tissues and have different functions. The isoform known as ALDH4A1 is primarily responsible for the conversion of alanine to pyruvate in the liver. Deficiencies or mutations in this enzyme can lead to a rare genetic disorder called 4-hydroxybutyric aciduria, which is characterized by elevated levels of 4-hydroxybutyric acid in the urine and neurological symptoms.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

11-Beta-Hydroxysteroid Dehydrogenase Type 1 (11β-HSD1) is an enzyme that plays a crucial role in the metabolism of steroid hormones, particularly cortisol, in the body. Cortisol is a glucocorticoid hormone produced by the adrenal glands that helps regulate various physiological processes such as metabolism, immune response, and stress response.

11β-HSD1 is primarily expressed in liver, fat, and muscle tissues, where it catalyzes the conversion of cortisone to cortisol. Cortisone is a biologically inactive form of cortisol that is produced when cortisol levels are high, and it needs to be converted back to cortisol for the hormone to exert its effects.

By increasing the availability of active cortisol in these tissues, 11β-HSD1 has been implicated in several metabolic disorders, including obesity, insulin resistance, and type 2 diabetes. Inhibitors of 11β-HSD1 are currently being investigated as potential therapeutic agents for the treatment of these conditions.

"Zymomonas" is a genus of Gram-negative, facultatively anaerobic bacteria that are commonly found in sugar-rich environments such as fruit and flower nectar. The most well-known species in this genus is Zymomonas mobilis, which has attracted significant interest in the field of biofuels research due to its ability to efficiently ferment sugars into ethanol.

Zymomonas bacteria are unique in their metabolism and possess a number of unusual features, including a highly streamlined genome, a single polar flagellum for motility, and the ability to survive and grow at relatively high temperatures and ethanol concentrations. These characteristics make Zymomonas an attractive candidate for industrial applications, particularly in the production of biofuels and other bioproducts.

In addition to their potential industrial uses, Zymomonas bacteria have also been implicated in certain human diseases, particularly in individuals with weakened immune systems or underlying medical conditions. However, such cases are relatively rare, and the overall impact of Zymomonas on human health is still not well understood.

Disulfiram is a medication used to treat chronic alcoholism. It works by inhibiting the enzyme acetaldehyde dehydrogenase, which is responsible for breaking down acetaldehyde, a toxic metabolite produced when alcohol is consumed. When a person taking disulfiram consumes alcohol, the buildup of acetaldehyde causes unpleasant symptoms such as flushing, nausea, palpitations, and shortness of breath, which can help discourage further alcohol use.

The medical definition of Disulfiram is:

A medication used in the treatment of chronic alcoholism, which works by inhibiting the enzyme acetaldehyde dehydrogenase, leading to an accumulation of acetaldehyde when alcohol is consumed, causing unpleasant symptoms that discourage further alcohol use. Disulfiram is available as a tablet for oral administration and is typically prescribed under medical supervision due to its potential for serious interactions with alcohol and other substances.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

Butylene glycols are a type of organic compounds that belong to the class of diols, which are chemical compounds containing two hydroxyl groups. Specifically, butylene glycols are composed of a four-carbon chain with two hydroxyl groups located on adjacent carbon atoms.

There are two isomeric forms of butylene glycol: 1,2-butanediol and 1,3-butanediol.

* 1,2-Butanediol (also known as 1,2-butylene glycol) has the hydroxyl groups on the first and second carbon atoms of the chain. It is a colorless, viscous liquid that is used as a solvent, humectant, and antifreeze in various industrial and cosmetic applications.
* 1,3-Butanediol (also known as 1,3-butylene glycol) has the hydroxyl groups on the first and third carbon atoms of the chain. It is also a colorless, viscous liquid that is used as a solvent, humectant, and antifreeze in various industrial and cosmetic applications.

Butylene glycols are generally considered to be safe for use in cosmetics and other consumer products, although they may cause skin irritation or allergic reactions in some individuals. They are also used as intermediates in the synthesis of other chemicals, such as polyesters and polyurethanes.

Fatty alcohols, also known as long-chain alcohols or long-chain fatty alcohols, are a type of fatty compound that contains a hydroxyl group (-OH) and a long alkyl chain. They are typically derived from natural sources such as plant and animal fats and oils, and can also be synthetically produced.

Fatty alcohols can vary in chain length, typically containing between 8 and 30 carbon atoms. They are commonly used in a variety of industrial and consumer products, including detergents, emulsifiers, lubricants, and personal care products. In the medical field, fatty alcohols may be used as ingredients in certain medications or topical treatments.

Species specificity is a term used in the field of biology, including medicine, to refer to the characteristic of a biological entity (such as a virus, bacterium, or other microorganism) that allows it to interact exclusively or preferentially with a particular species. This means that the biological entity has a strong affinity for, or is only able to infect, a specific host species.

For example, HIV is specifically adapted to infect human cells and does not typically infect other animal species. Similarly, some bacterial toxins are species-specific and can only affect certain types of animals or humans. This concept is important in understanding the transmission dynamics and host range of various pathogens, as well as in developing targeted therapies and vaccines.

Hexanols are a class of organic compounds that contain a hexanol functional group, which is a hydroxyl group (-OH) attached to a linear or branched carbon chain containing six carbon atoms. They can be either primary, secondary, or tertiary alcohols depending on the position of the hydroxyl group in relation to the carbon chain. Hexanols are used in various applications such as in the production of flavors, fragrances, and industrial chemicals.

Hydroxyprostaglandin Dehydrogenases (HPGDs) are a group of enzymes that catalyze the oxidation of prostaglandins, which are hormone-like lipid compounds with various physiological effects in the body. The oxidation reaction catalyzed by HPGDs involves the removal of hydrogen atoms from the prostaglandin molecule and the addition of a ketone group in its place.

The HPGD family includes several isoforms, each with distinct tissue distributions and substrate specificities. The most well-known isoform is 15-hydroxyprostaglandin dehydrogenase (15-PGDH), which preferentially oxidizes PGE2 and PGF2α at the 15-hydroxyl position, thereby inactivating these prostaglandins.

The regulation of HPGD activity is critical for maintaining prostaglandin homeostasis, as imbalances in prostaglandin levels have been linked to various pathological conditions, including inflammation, cancer, and cardiovascular disease. For example, decreased 15-PGDH expression has been observed in several types of cancer, leading to increased PGE2 levels and promoting tumor growth and progression.

Overall, Hydroxyprostaglandin Dehydrogenases play a crucial role in regulating prostaglandin signaling and have important implications for human health and disease.

Hydroxysteroids are steroid hormones or steroid compounds that contain one or more hydroxyl groups (-OH) as a functional group. These molecules have a steroid nucleus, which is a core structure composed of four fused carbon rings, and one or more hydroxyl groups attached to the rings.

The presence of hydroxyl groups makes hydroxysteroids polar and more soluble in water compared to other steroids. They are involved in various physiological processes, such as metabolism, bile acid synthesis, and steroid hormone regulation. Some examples of hydroxysteroids include certain forms of estrogens, androgens, corticosteroids, and bile acids.

It is important to note that the specific medical definition may vary depending on the context or source.

Octanols are a type of chemical compound known as alcohols, specifically they are fatty alcohols with a chain of 8 carbon atoms. The most common octanol is called 1-octanol, which has the chemical formula CH3(CH2)7OH. It is a colorless oily liquid that is used in the synthesis of other chemicals and as a solvent. Octanols are often used as standards for measuring the partition coefficient between octanol and water, which is a measure of a compound's hydrophobicity or lipophilicity. This property is important in understanding how a compound may be absorbed, distributed, metabolized, and excreted in the body.

According to the Diagnostic and Statistical Manual of Mental Disorders, Fifth Edition (DSM-5), alcohol-related disorders are a category of mental disorders defined by a problematic pattern of alcohol use that leads to clinically significant impairment or distress. The disorders include:

1. Alcohol Use Disorder (AUD): A chronic relapsing brain disorder characterized by an impaired ability to stop or control alcohol use despite adverse social, occupational, or health consequences. AUD can be mild, moderate, or severe, and recovery is possible regardless of severity. The symptoms include problems controlling intake of alcohol, continued use despite problems resulting from drinking, development of a tolerance, drinking that leads to risky situations, or withdrawal symptoms when not drinking.
2. Alcohol Intoxication: A state of acute impairment in mental and motor function caused by the recent consumption of alcohol. The symptoms include slurred speech, unsteady gait, nystagmus, impaired attention or memory, stupor, or coma. In severe cases, it can lead to respiratory depression, hypothermia, or even death.
3. Alcohol Withdrawal: A syndrome that occurs when alcohol use is heavily reduced or stopped after prolonged and heavy use. The symptoms include autonomic hyperactivity, increased hand tremor, insomnia, nausea or vomiting, transient visual, tactile, or auditory hallucinations or illusions, psychomotor agitation, anxiety, and grand mal seizures.
4. Other Alcohol-Induced Disorders: These include alcohol-induced sleep disorder, alcohol-induced sexual dysfunction, and alcohol-induced major neurocognitive disorder.

It is important to note that alcohol use disorders are complex conditions that can be influenced by a variety of factors, including genetics, environment, and personal behavior. If you or someone you know is struggling with alcohol use, it is recommended to seek professional help.

Spectrophotometry is a technical analytical method used in the field of medicine and science to measure the amount of light absorbed or transmitted by a substance at specific wavelengths. This technique involves the use of a spectrophotometer, an instrument that measures the intensity of light as it passes through a sample.

In medical applications, spectrophotometry is often used in laboratory settings to analyze various biological samples such as blood, urine, and tissues. For example, it can be used to measure the concentration of specific chemicals or compounds in a sample by measuring the amount of light that is absorbed or transmitted at specific wavelengths.

In addition, spectrophotometry can also be used to assess the properties of biological tissues, such as their optical density and thickness. This information can be useful in the diagnosis and treatment of various medical conditions, including skin disorders, eye diseases, and cancer.

Overall, spectrophotometry is a valuable tool for medical professionals and researchers seeking to understand the composition and properties of various biological samples and tissues.

Butyryl-CoA dehydrogenase (BD) is an enzyme that plays a crucial role in the breakdown and metabolism of fatty acids, specifically those with medium chain length. It catalyzes the oxidation of butyryl-CoA to crotonyl-CoA, which is an important step in the beta-oxidation pathway.

The reaction catalyzed by BD can be summarized as follows:

butyryl-CoA + FAD → crotonyl-CoA + FADH2 + CO2

In this reaction, butyryl-CoA is oxidized to crotonyl-CoA, and FAD (flavin adenine dinucleotide) is reduced to FADH2. The release of CO2 is a byproduct of the reaction.

BD is an important enzyme in energy metabolism, as it helps to generate reducing equivalents that can be used in the electron transport chain to produce ATP, the primary source of cellular energy. Deficiencies in BD have been linked to various metabolic disorders, including a rare genetic disorder known as multiple acyl-CoA dehydrogenase deficiency (MADD), which is characterized by impaired fatty acid and amino acid metabolism.

'Acinetobacter calcoaceticus' is a species of gram-negative, aerobic bacteria that is commonly found in the environment, such as in soil and water. It is a non-motile, oxidase-negative organism that can form biofilms and has the ability to survive in a wide range of temperatures and pH levels.

While 'Acinetobacter calcoaceticus' itself is generally considered to be a low-virulence bacterium, it is closely related to other species within the genus 'Acinetobacter' that are known to cause healthcare-associated infections, particularly in immunocompromised patients or those with underlying medical conditions. These infections can include pneumonia, bloodstream infections, meningitis, and wound infections.

It is important to note that the identification of 'Acinetobacter calcoaceticus' can be challenging due to its tendency to form mixed cultures with other 'Acinetobacter' species, as well as its ability to undergo genetic changes that can make it difficult to distinguish from other members of the genus. Accurate identification and antimicrobial susceptibility testing are critical for appropriate treatment and infection control measures.

Ketones are organic compounds that contain a carbon atom bound to two oxygen atoms and a central carbon atom bonded to two additional carbon groups through single bonds. In the context of human physiology, ketones are primarily produced as byproducts when the body breaks down fat for energy in a process called ketosis.

Specifically, under conditions of low carbohydrate availability or prolonged fasting, the liver converts fatty acids into ketone bodies, which can then be used as an alternative fuel source for the brain and other organs. The three main types of ketones produced in the human body are acetoacetate, beta-hydroxybutyrate, and acetone.

Elevated levels of ketones in the blood, known as ketonemia, can occur in various medical conditions such as diabetes, starvation, alcoholism, and high-fat/low-carbohydrate diets. While moderate levels of ketosis are generally considered safe, severe ketosis can lead to a life-threatening condition called diabetic ketoacidosis (DKA) in people with diabetes.

A gene is a specific sequence of nucleotides in DNA that carries genetic information. Genes are the fundamental units of heredity and are responsible for the development and function of all living organisms. They code for proteins or RNA molecules, which carry out various functions within cells and are essential for the structure, function, and regulation of the body's tissues and organs.

Each gene has a specific location on a chromosome, and each person inherits two copies of every gene, one from each parent. Variations in the sequence of nucleotides in a gene can lead to differences in traits between individuals, including physical characteristics, susceptibility to disease, and responses to environmental factors.

Medical genetics is the study of genes and their role in health and disease. It involves understanding how genes contribute to the development and progression of various medical conditions, as well as identifying genetic risk factors and developing strategies for prevention, diagnosis, and treatment.

A bacterial gene is a segment of DNA (or RNA in some viruses) that contains the genetic information necessary for the synthesis of a functional bacterial protein or RNA molecule. These genes are responsible for encoding various characteristics and functions of bacteria such as metabolism, reproduction, and resistance to antibiotics. They can be transmitted between bacteria through horizontal gene transfer mechanisms like conjugation, transformation, and transduction. Bacterial genes are often organized into operons, which are clusters of genes that are transcribed together as a single mRNA molecule.

It's important to note that the term "bacterial gene" is used to describe genetic elements found in bacteria, but not all genetic elements in bacteria are considered genes. For example, some DNA sequences may not encode functional products and are therefore not considered genes. Additionally, some bacterial genes may be plasmid-borne or phage-borne, rather than being located on the bacterial chromosome.

Alcohol deterrents, also known as alcohol deterrent devices or ignition interlock devices, are breathalyzer devices that are installed in vehicles to prevent a driver from starting the vehicle if their blood alcohol concentration (BAC) is above a certain limit. These devices are often used as a condition of license reinstatement for individuals who have been convicted of drunk driving or other alcohol-related offenses.

The driver must blow into the device, and if their BAC is above the programmed limit, the vehicle will not start. Some devices also require periodic rolling retests while the vehicle is in motion to ensure that the driver remains sober throughout the trip. The use of alcohol deterrents has been shown to reduce recidivism rates among drunk drivers and improve overall road safety.

Anaerobiosis is a state in which an organism or a portion of an organism is able to live and grow in the absence of molecular oxygen (O2). In biological contexts, "anaerobe" refers to any organism that does not require oxygen for growth, and "aerobe" refers to an organism that does require oxygen for growth.

There are two types of anaerobes: obligate anaerobes, which cannot tolerate the presence of oxygen and will die if exposed to it; and facultative anaerobes, which can grow with or without oxygen but prefer to grow in its absence. Some organisms are able to switch between aerobic and anaerobic metabolism depending on the availability of oxygen, a process known as "facultative anaerobiosis."

Anaerobic respiration is a type of metabolic process that occurs in the absence of molecular oxygen. In this process, organisms use alternative electron acceptors other than oxygen to generate energy through the transfer of electrons during cellular respiration. Examples of alternative electron acceptors include nitrate, sulfate, and carbon dioxide.

Anaerobic metabolism is less efficient than aerobic metabolism in terms of energy production, but it allows organisms to survive in environments where oxygen is not available or is toxic. Anaerobic bacteria are important decomposers in many ecosystems, breaking down organic matter and releasing nutrients back into the environment. In the human body, anaerobic bacteria can cause infections and other health problems if they proliferate in areas with low oxygen levels, such as the mouth, intestines, or deep tissue wounds.

20-Hydroxysteroid Dehydrogenases (20-HSDs) are a group of enzymes that play a crucial role in the metabolism of steroid hormones. These enzymes catalyze the conversion of steroid hormone precursors to their active forms by adding or removing a hydroxyl group at the 20th carbon position of the steroid molecule.

There are several isoforms of 20-HSDs, each with distinct tissue distribution and substrate specificity. The most well-known isoforms include 20-HSD type I and II, which have opposing functions in regulating the activity of cortisol, a glucocorticoid hormone produced by the adrenal gland.

Type I 20-HSD, primarily found in the liver and adipose tissue, converts inactive cortisone to its active form, cortisol. In contrast, type II 20-HSD, expressed mainly in the kidney, brain, and immune cells, catalyzes the reverse reaction, converting cortisol back to cortisone.

Dysregulation of 20-HSDs has been implicated in various medical conditions, such as metabolic disorders, inflammatory diseases, and cancers. Therefore, understanding the function and regulation of these enzymes is essential for developing targeted therapies for these conditions.

2-Propanol is a type of alcohol, also known as isopropanol or isopropyl alcohol. It is a colorless, flammable liquid with a characteristic odor. 2-Propanol is miscible with water and most organic solvents.

It is commonly used as a solvent and as an antiseptic or disinfectant, due to its ability to denature proteins and disrupt microbial cell membranes. In medical settings, 2-Propanol is often used as a skin sanitizer or hand rub to reduce the number of microorganisms on the skin.

Ingestion or prolonged exposure to 2-Propanol can cause irritation to the eyes, skin, and respiratory tract, and may lead to central nervous system depression, nausea, vomiting, and other symptoms. It is important to handle 2-Propanol with care and follow appropriate safety precautions when using it.

Acetone is a colorless, volatile, and flammable liquid organic compound with the chemical formula (CH3)2CO. It is the simplest and smallest ketone, and its molecules consist of a carbonyl group linked to two methyl groups. Acetone occurs naturally in the human body and is produced as a byproduct of normal metabolic processes, particularly during fat burning.

In clinical settings, acetone can be measured in breath or blood to assess metabolic status, such as in cases of diabetic ketoacidosis, where an excess production of acetone and other ketones occurs due to insulin deficiency and high levels of fatty acid breakdown. High concentrations of acetone can lead to a sweet, fruity odor on the breath, often described as "fruity acetone" or "acetone breath."

Multienzyme complexes are specialized protein structures that consist of multiple enzymes closely associated or bound together, often with other cofactors and regulatory subunits. These complexes facilitate the sequential transfer of substrates along a series of enzymatic reactions, also known as a metabolic pathway. By keeping the enzymes in close proximity, multienzyme complexes enhance reaction efficiency, improve substrate specificity, and maintain proper stoichiometry between different enzymes involved in the pathway. Examples of multienzyme complexes include the pyruvate dehydrogenase complex, the citrate synthase complex, and the fatty acid synthetase complex.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

'Acinetobacter' is a genus of gram-negative, aerobic bacteria that are commonly found in the environment, including water, soil, and healthcare settings. They are known for their ability to survive in a wide range of temperatures and pH levels, as well as their resistance to many antibiotics.

Some species of Acinetobacter can cause healthcare-associated infections, particularly in patients who are hospitalized, have weakened immune systems, or have been exposed to medical devices such as ventilators or catheters. These infections can include pneumonia, bloodstream infections, wound infections, and meningitis.

Acinetobacter baumannii is one of the most common species associated with human infection and is often resistant to multiple antibiotics, making it a significant public health concern. Infections caused by Acinetobacter can be difficult to treat and may require the use of last-resort antibiotics.

Preventing the spread of Acinetobacter in healthcare settings is important and includes practices such as hand hygiene, environmental cleaning, and contact precautions for patients with known or suspected infection.

In the context of medicine, "chemistry" often refers to the field of study concerned with the properties, composition, and structure of elements and compounds, as well as their reactions with one another. It is a fundamental science that underlies much of modern medicine, including pharmacology (the study of drugs), toxicology (the study of poisons), and biochemistry (the study of the chemical processes that occur within living organisms).

In addition to its role as a basic science, chemistry is also used in medical testing and diagnosis. For example, clinical chemistry involves the analysis of bodily fluids such as blood and urine to detect and measure various substances, such as glucose, cholesterol, and electrolytes, that can provide important information about a person's health status.

Overall, chemistry plays a critical role in understanding the mechanisms of diseases, developing new treatments, and improving diagnostic tests and techniques.

11-Beta-Hydroxysteroid Dehydrogenase Type 2 (11β-HSD2) is an enzyme that plays a crucial role in the regulation of steroid hormones, particularly cortisol and aldosterone. It is primarily found in tissues such as the kidneys, colon, and salivary glands.

The main function of 11β-HSD2 is to convert active cortisol into inactive cortisone, which helps to prevent excessive mineralocorticoid receptor activation by cortisol. This is important because cortisol can bind to and activate mineralocorticoid receptors, leading to increased sodium reabsorption and potassium excretion in the kidneys, as well as other effects on blood pressure and electrolyte balance.

By converting cortisol to cortisone, 11β-HSD2 helps to protect mineralocorticoid receptors from being overstimulated by cortisol, allowing aldosterone to bind and activate these receptors instead. This is important for maintaining normal blood pressure and electrolyte balance.

Deficiencies or mutations in the 11β-HSD2 enzyme can lead to a condition called apparent mineralocorticoid excess (AME), which is characterized by high blood pressure, low potassium levels, and increased sodium reabsorption in the kidneys. This occurs because cortisol is able to bind to and activate mineralocorticoid receptors in the absence of 11β-HSD2 activity.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

Chemical phenomena refer to the changes and interactions that occur at the molecular or atomic level when chemicals are involved. These phenomena can include chemical reactions, in which one or more substances (reactants) are converted into different substances (products), as well as physical properties that change as a result of chemical interactions, such as color, state of matter, and solubility. Chemical phenomena can be studied through various scientific disciplines, including chemistry, biochemistry, and physics.

I'm sorry for any confusion, but "Polyvinyl Alcohol" is not a medical term. It is a chemical compound used in various industrial and commercial applications, including the production of adhesives, paints, and medical devices. Polyvinyl Alcohol is a type of synthetic polymer made from the polymerization of vinyl acetate monomer, followed by alcoholysis to replace the acetate groups with hydroxyl groups.

In a medical context, Polyvinyl Alcohol might be used in certain medical devices or applications, such as contact lenses, eye drops, and drug delivery systems, due to its biocompatibility and resistance to protein absorption. However, it is not a term commonly used to describe a medical condition or treatment.

Immobilized enzymes refer to enzymes that have been restricted or fixed in a specific location and are unable to move freely. This is typically achieved through physical or chemical methods that attach the enzyme to a solid support or matrix. The immobilization of enzymes can provide several advantages, including increased stability, reusability, and ease of separation from the reaction mixture.

Immobilized enzymes are widely used in various industrial applications, such as biotransformations, biosensors, and diagnostic kits. They can also be used for the production of pharmaceuticals, food additives, and other fine chemicals. The immobilization techniques include adsorption, covalent binding, entrapment, and cross-linking.

Adsorption involves physically attaching the enzyme to a solid support through weak forces such as van der Waals interactions or hydrogen bonding. Covalent binding involves forming chemical bonds between the enzyme and the support matrix. Entrapment involves encapsulating the enzyme within a porous matrix, while cross-linking involves chemically linking multiple enzyme molecules together to form a stable structure.

Overall, immobilized enzymes offer several advantages over free enzymes, including improved stability, reusability, and ease of separation from the reaction mixture, making them valuable tools in various industrial applications.

Acyl-CoA dehydrogenase, long-chain (LCHAD) is a medical term that refers to an enzyme found in the body that plays a crucial role in breaking down fatty acids for energy. This enzyme is responsible for catalyzing the first step in the beta-oxidation of long-chain fatty acids, which involves the removal of hydrogen atoms from the fatty acid molecule to create a double bond.

Mutations in the gene that encodes LCHAD can lead to deficiencies in the enzyme's activity, resulting in an accumulation of unmetabolized long-chain fatty acids in the body. This can cause a range of symptoms, including hypoglycemia (low blood sugar), muscle weakness, and liver dysfunction. In severe cases, LCHAD deficiency can lead to serious complications such as heart problems, developmental delays, and even death.

LCHAD deficiency is typically diagnosed through newborn screening or genetic testing, and treatment may involve dietary modifications, supplementation with medium-chain triglycerides (MCTs), and avoidance of fasting to prevent the breakdown of fatty acids for energy. In some cases, LCHAD deficiency may require more intensive treatments such as carnitine supplementation or liver transplantation.

I'm sorry for any confusion, but "Formates" is not a recognized term in medical terminology. It is possible that you may be referring to "formic acid" or "formate," which are terms used in chemistry and biochemistry. Formic acid is a colorless, pungent, and corrosive liquid with the chemical formula HCOOH. Its salts are called formates.

Formate is the anion (negatively charged ion) of formic acid, with the chemical formula HCOO-. Formate can be found in various biological systems and is involved in several metabolic processes. If you could provide more context or clarify your question, I would be happy to help further.

Homoserine dehydrogenase is an enzyme involved in the metabolism of certain amino acids. Specifically, it catalyzes the conversion of homoserine to aspartate semialdehyde, which is a key step in the biosynthesis of several essential amino acids, including threonine, methionine, and isoleucine. The reaction catalyzed by homoserine dehydrogenase involves the oxidation of homoserine to form aspartate semialdehyde, using NAD or NADP as a cofactor. There are several isoforms of this enzyme found in different organisms, and it has been studied extensively due to its importance in amino acid metabolism and potential as a target for antibiotic development.

Iodoacetates are salts or esters of iodoacetic acid, an organic compound containing iodine. In medicine, iodoacetates have been used as topical antiseptics and anti-inflammatory agents. However, their use is limited due to potential skin irritation and the availability of safer alternatives.

In a broader context, iodoacetates are also known for their chemical properties. They can act as alkylating agents, which means they can react with proteins and enzymes in living organisms, disrupting their function. This property has been exploited in research to study various cellular processes.

Temperature, in a medical context, is a measure of the degree of hotness or coldness of a body or environment. It is usually measured using a thermometer and reported in degrees Celsius (°C), degrees Fahrenheit (°F), or kelvin (K). In the human body, normal core temperature ranges from about 36.5-37.5°C (97.7-99.5°F) when measured rectally, and can vary slightly depending on factors such as time of day, physical activity, and menstrual cycle. Elevated body temperature is a common sign of infection or inflammation, while abnormally low body temperature can indicate hypothermia or other medical conditions.

"Pseudomonas putida" is a species of gram-negative, rod-shaped bacteria that is commonly found in soil and water environments. It is a non-pathogenic, opportunistic microorganism that is known for its versatile metabolism and ability to degrade various organic compounds. This bacterium has been widely studied for its potential applications in bioremediation and industrial biotechnology due to its ability to break down pollutants such as toluene, xylene, and other aromatic hydrocarbons. It is also known for its resistance to heavy metals and antibiotics, making it a valuable tool in the study of bacterial survival mechanisms and potential applications in bioremediation and waste treatment.

Isovaleryl-CoA Dehydrogenase (IVD) is an enzyme that plays a crucial role in the catabolism of leucine, an essential amino acid. This enzyme is located in the mitochondrial matrix and is responsible for catalyzing the third step in the degradation pathway of leucine.

Specifically, Isovaleryl-CoA Dehydrogenase facilitates the conversion of isovaleryl-CoA to 3-methylcrotonyl-CoA through the removal of two hydrogen atoms from the substrate. This reaction requires the coenzyme flavin adenine dinucleotide (FAD) as an electron acceptor, which gets reduced to FADH2 during the process.

Deficiency in Isovaleryl-CoA Dehydrogenase can lead to a rare genetic disorder known as isovaleric acidemia, characterized by the accumulation of isovaleryl-CoA and its metabolic byproducts, including isovaleric acid, 3-hydroxyisovaleric acid, and methylcrotonylglycine. These metabolites can cause various symptoms such as vomiting, dehydration, metabolic acidosis, seizures, developmental delay, and even coma or death in severe cases.

3-Isopropylmalate dehydrogenase (IPMDH) is an enzyme that plays a crucial role in the metabolic pathway known as leucine biosynthesis. This enzyme catalyzes the third step of this pathway, which involves the oxidative decarboxylation of 3-isopropylmalate to form 2-isopropylmalate, while simultaneously reducing NAD+ to NADH. The reaction is as follows:

3-Isopropylmalate + NAD+ -> 2-isopropylmalate + CO2 + NADH

The IPMDH enzyme is found in various organisms, including bacteria, yeast, and plants. In humans, defects or mutations in the gene encoding this enzyme can lead to a rare genetic disorder called 3-isopropylmalate dehydrogenase deficiency. This condition results in elevated levels of leucine and other intermediates in the leucine biosynthesis pathway, which can cause neurological symptoms such as developmental delay, seizures, and hypotonia (low muscle tone).

I'm sorry for any confusion, but "Mandelic Acids" is not a recognized medical term or concept in dermatology or medicine. Mandelic acid, however, is a type of chemical compound used in skincare products for various purposes such as exfoliation and reducing hyperpigmentation. It is an aromatic hydroxyacetic acid derived from mandelic almonds. If you have any questions about skincare ingredients or treatments, I'd be happy to help clarify those for you!

Pyrazoles are heterocyclic aromatic organic compounds that contain a six-membered ring with two nitrogen atoms at positions 1 and 2. The chemical structure of pyrazoles consists of a pair of nitrogen atoms adjacent to each other in the ring, which makes them unique from other azole heterocycles such as imidazoles or triazoles.

Pyrazoles have significant biological activities and are found in various pharmaceuticals, agrochemicals, and natural products. Some pyrazole derivatives exhibit anti-inflammatory, analgesic, antipyretic, antimicrobial, antiviral, antifungal, and anticancer properties.

In the medical field, pyrazoles are used in various drugs to treat different conditions. For example, celecoxib (Celebrex) is a selective COX-2 inhibitor used for pain relief and inflammation reduction in arthritis patients. It contains a pyrazole ring as its core structure. Similarly, febuxostat (Uloric) is a medication used to treat gout, which also has a pyrazole moiety.

Overall, pyrazoles are essential compounds with significant medical applications and potential for further development in drug discovery and design.

Cortisone reductase is not a widely used medical term, but it generally refers to an enzyme that converts cortisone to its active form, cortisol. Cortisol is a steroid hormone produced by the adrenal gland that helps regulate metabolism and helps your body respond to stress. The enzyme responsible for this conversion is specifically called 11β-hydroxysteroid dehydrogenase type 1 (11β-HSD1).

There are two types of 11β-HSD enzymes: 11β-HSD1 and 11β-HSD2. While 11β-HSD1 acts as a reductase, converting cortisone to cortisol, 11β-HSD2 has an opposing function, working as a dehydrogenase that converts cortisol to cortisone. These enzymes play crucial roles in maintaining the balance of cortisol levels in the body and are involved in various physiological processes.

It is important to note that 'cortisone reductase' may not be a term commonly used by medical professionals, and it might be more appropriate to refer to the enzyme as 11β-HSD1 for clarity and precision.

Phylogeny is the evolutionary history and relationship among biological entities, such as species or genes, based on their shared characteristics. In other words, it refers to the branching pattern of evolution that shows how various organisms have descended from a common ancestor over time. Phylogenetic analysis involves constructing a tree-like diagram called a phylogenetic tree, which depicts the inferred evolutionary relationships among organisms or genes based on molecular sequence data or other types of characters. This information is crucial for understanding the diversity and distribution of life on Earth, as well as for studying the emergence and spread of diseases.

Tert-butyl alcohol, also known as t-butanol or 2-methylpropan-2-ol, is not a medication or a substance used in medical treatments. Therefore, it does not have a specific medical definition. However, I can provide you with a general chemical definition:

Tert-butyl alcohol is a primary alcohol with the molecular formula (CH3)3COH. It is a colorless and flammable liquid with a characteristic camphor-like odor. Tert-butyl alcohol is used as a solvent, denaturant for alcohols, and an intermediate in chemical synthesis. It is less toxic than other common alcohols like ethanol or methanol, but it can still cause irritation to the eyes, skin, and respiratory tract.

Leucine dehydrogenase (LDH) is an enzyme that catalyzes the reversible conversion of leucine to α-ketoisocaproate, while simultaneously reducing NAD+ to NADH. It plays a crucial role in the metabolism of branched-chain amino acids and is widely distributed in various tissues such as liver, kidney, heart, skeletal muscle, and brain.

In clinical settings, LDH is often measured in serum or plasma as a biomarker for tissue damage since it is released into the bloodstream upon cell death or injury. Elevated levels of LDH can be observed in various conditions such as myocardial infarction, hemolysis, liver disease, muscle damage, and some types of cancer. However, an isolated increase in LDH may not be specific to a particular condition, and further diagnostic tests are usually required for accurate diagnosis.

Phosphoglycerate Dehydrogenase (PGDH) is a critical enzyme in the metabolic pathway of glycolysis and serine synthesis. It catalyzes the first step in the serine synthesis pathway, where 3-phosphoglycerate is converted to 3-phosphohydroxypyruvate, while also reducing nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide hydride (NADH). This enzyme plays a significant role in cellular metabolism and has been linked to various diseases, including cancer, when its activity is dysregulated.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Restriction mapping is a technique used in molecular biology to identify the location and arrangement of specific restriction endonuclease recognition sites within a DNA molecule. Restriction endonucleases are enzymes that cut double-stranded DNA at specific sequences, producing fragments of various lengths. By digesting the DNA with different combinations of these enzymes and analyzing the resulting fragment sizes through techniques such as agarose gel electrophoresis, researchers can generate a restriction map - a visual representation of the locations and distances between recognition sites on the DNA molecule. This information is crucial for various applications, including cloning, genome analysis, and genetic engineering.

Propylene glycol is not a medical term, but rather a chemical compound. However, it does have various applications in the medical field. Medically, propylene glycol can be used as a:

1. Vehicle for intravenous (IV) medications: Propylene glycol helps dissolve drugs that are not water-soluble and allows them to be administered intravenously. It is used in the preparation of some IV medications, including certain antibiotics, antivirals, and chemotherapeutic agents.
2. Preservative: Propylene glycol acts as a preservative in various medical products, such as topical ointments, eye drops, and injectable solutions, to prevent bacterial growth and increase shelf life.
3. Humectant: In some medical devices and pharmaceutical formulations, propylene glycol is used as a humectant, which means it helps maintain moisture and prevent dryness in the skin or mucous membranes.

The chemical definition of propylene glycol (C3H8O2) is:

A colorless, nearly odorless, viscous liquid belonging to the alcohol family. It is a diol, meaning it contains two hydroxyl groups (-OH), and its molecular formula is C3H8O2. Propylene glycol is miscible with water and most organic solvents and has applications in various industries, including pharmaceuticals, food processing, cosmetics, and industrial manufacturing.

Spectrophotometry, Ultraviolet (UV-Vis) is a type of spectrophotometry that measures how much ultraviolet (UV) and visible light is absorbed or transmitted by a sample. It uses a device called a spectrophotometer to measure the intensity of light at different wavelengths as it passes through a sample. The resulting data can be used to determine the concentration of specific components within the sample, identify unknown substances, or evaluate the physical and chemical properties of materials.

UV-Vis spectroscopy is widely used in various fields such as chemistry, biology, pharmaceuticals, and environmental science. It can detect a wide range of substances including organic compounds, metal ions, proteins, nucleic acids, and dyes. The technique is non-destructive, meaning that the sample remains unchanged after the measurement.

In UV-Vis spectroscopy, the sample is placed in a cuvette or other container, and light from a source is directed through it. The light then passes through a monochromator, which separates it into its component wavelengths. The monochromatic light is then directed through the sample, and the intensity of the transmitted or absorbed light is measured by a detector.

The resulting absorption spectrum can provide information about the concentration and identity of the components in the sample. For example, if a compound has a known absorption maximum at a specific wavelength, its concentration can be determined by measuring the absorbance at that wavelength and comparing it to a standard curve.

Overall, UV-Vis spectrophotometry is a versatile and powerful analytical technique for quantitative and qualitative analysis of various samples in different fields.

Pyruvate is a negatively charged ion or group of atoms, called anion, with the chemical formula C3H3O3-. It is formed from the decomposition of glucose and other sugars in the process of cellular respiration. Pyruvate plays a crucial role in the metabolic pathways that generate energy for cells.

In the cytoplasm, pyruvate is produced through glycolysis, where one molecule of glucose is broken down into two molecules of pyruvate, releasing energy and producing ATP (adenosine triphosphate) and NADH (reduced nicotinamide adenine dinucleotide).

In the mitochondria, pyruvate can be further metabolized through the citric acid cycle (also known as the Krebs cycle) to produce more ATP. The process involves the conversion of pyruvate into acetyl-CoA, which then enters the citric acid cycle and undergoes a series of reactions that generate energy in the form of ATP, NADH, and FADH2 (reduced flavin adenine dinucleotide).

Overall, pyruvate is an important intermediate in cellular respiration and plays a central role in the production of energy for cells.

Estradiol dehydrogenases are a group of enzymes that are involved in the metabolism of estradiols, which are steroid hormones that play important roles in the development and maintenance of female reproductive system and secondary sexual characteristics. These enzymes catalyze the oxidation or reduction reactions of estradiols, converting them to other forms of steroid hormones.

There are two main types of estradiol dehydrogenases: 1) 3-alpha-hydroxysteroid dehydrogenase (3-alpha HSD), which catalyzes the conversion of estradi-17-beta to estrone, and 2) 17-beta-hydroxysteroid dehydrogenase (17-beta HSD), which catalyzes the reverse reaction, converting estrone back to estradiol.

These enzymes are widely distributed in various tissues, including the ovaries, placenta, liver, and adipose tissue, and play important roles in regulating the levels of estradiols in the body. Abnormalities in the activity of these enzymes have been associated with several medical conditions, such as hormone-dependent cancers, polycystic ovary syndrome, and hirsutism.

Sequence homology in nucleic acids refers to the similarity or identity between the nucleotide sequences of two or more DNA or RNA molecules. It is often used as a measure of biological relationship between genes, organisms, or populations. High sequence homology suggests a recent common ancestry or functional constraint, while low sequence homology may indicate a more distant relationship or different functions.

Nucleic acid sequence homology can be determined by various methods such as pairwise alignment, multiple sequence alignment, and statistical analysis. The degree of homology is typically expressed as a percentage of identical or similar nucleotides in a given window of comparison.

It's important to note that the interpretation of sequence homology depends on the biological context and the evolutionary distance between the sequences compared. Therefore, functional and experimental validation is often necessary to confirm the significance of sequence homology.

Benzyl compounds are organic chemical compounds that contain a benzyl group, which is a functional group consisting of a carbon atom attached to a CH3 group (methyl group) and an aromatic ring, usually a phenyl group. The benzyl group can be represented as -CH2-C6H5.

Benzyl compounds have various applications in different fields such as pharmaceuticals, flavors, fragrances, dyes, and polymers. In pharmaceuticals, benzyl compounds are used as active ingredients or intermediates in the synthesis of drugs. For example, benzylpenicillin is a widely used antibiotic that contains a benzyl group.

Benzyl alcohol, benzyl chloride, and benzyl acetate are some common examples of benzyl compounds with various industrial applications. Benzyl alcohol is used as a solvent, preservative, and intermediate in the synthesis of other chemicals. Benzyl chloride is an important chemical used in the production of resins, dyes, and pharmaceuticals. Benzyl acetate is used as a flavoring agent and fragrance in food and cosmetic products.

It's worth noting that benzyl compounds can be toxic or harmful if ingested, inhaled, or come into contact with the skin, depending on their chemical properties and concentrations. Therefore, they should be handled with care and used under appropriate safety measures.

A plasmid is a small, circular, double-stranded DNA molecule that is separate from the chromosomal DNA of a bacterium or other organism. Plasmids are typically not essential for the survival of the organism, but they can confer beneficial traits such as antibiotic resistance or the ability to degrade certain types of pollutants.

Plasmids are capable of replicating independently of the chromosomal DNA and can be transferred between bacteria through a process called conjugation. They often contain genes that provide resistance to antibiotics, heavy metals, and other environmental stressors. Plasmids have also been engineered for use in molecular biology as cloning vectors, allowing scientists to replicate and manipulate specific DNA sequences.

Plasmids are important tools in genetic engineering and biotechnology because they can be easily manipulated and transferred between organisms. They have been used to produce vaccines, diagnostic tests, and genetically modified organisms (GMOs) for various applications, including agriculture, medicine, and industry.

D-Xylulose Reductase is an enzyme that catalyzes the reduction of D-xylulose to xylitol using NADPH as a cofactor. This enzyme plays a role in the pentose phosphate pathway, which is a metabolic pathway that supplies reducing energy to cells by maintaining the level of the coenzyme NADPH. D-Xylulose Reductase is also involved in the metabolism of xylose, a type of sugar found in some fruits and vegetables, and is therefore of interest in the development of processes for the conversion of xylose to xylitol, a sweetener used in various food and pharmaceutical applications.

Bacterial proteins are a type of protein that are produced by bacteria as part of their structural or functional components. These proteins can be involved in various cellular processes, such as metabolism, DNA replication, transcription, and translation. They can also play a role in bacterial pathogenesis, helping the bacteria to evade the host's immune system, acquire nutrients, and multiply within the host.

Bacterial proteins can be classified into different categories based on their function, such as:

1. Enzymes: Proteins that catalyze chemical reactions in the bacterial cell.
2. Structural proteins: Proteins that provide structural support and maintain the shape of the bacterial cell.
3. Signaling proteins: Proteins that help bacteria to communicate with each other and coordinate their behavior.
4. Transport proteins: Proteins that facilitate the movement of molecules across the bacterial cell membrane.
5. Toxins: Proteins that are produced by pathogenic bacteria to damage host cells and promote infection.
6. Surface proteins: Proteins that are located on the surface of the bacterial cell and interact with the environment or host cells.

Understanding the structure and function of bacterial proteins is important for developing new antibiotics, vaccines, and other therapeutic strategies to combat bacterial infections.

Fluorescence spectrometry is a type of analytical technique used to investigate the fluorescent properties of a sample. It involves the measurement of the intensity of light emitted by a substance when it absorbs light at a specific wavelength and then re-emits it at a longer wavelength. This process, known as fluorescence, occurs because the absorbed energy excites electrons in the molecules of the substance to higher energy states, and when these electrons return to their ground state, they release the excess energy as light.

Fluorescence spectrometry typically measures the emission spectrum of a sample, which is a plot of the intensity of emitted light versus the wavelength of emission. This technique can be used to identify and quantify the presence of specific fluorescent molecules in a sample, as well as to study their photophysical properties.

Fluorescence spectrometry has many applications in fields such as biochemistry, environmental science, and materials science. For example, it can be used to detect and measure the concentration of pollutants in water samples, to analyze the composition of complex biological mixtures, or to study the properties of fluorescent nanomaterials.

"Thermoanaerobacter" is a genus of bacteria that are thermophilic (grow optimally at higher temperatures), anaerobic (do not require oxygen for growth), and straight or slightly curved rods in shape. They are capable of fermenting various sugars, organic acids, and alcohols to produce energy, with the formation of end products such as hydrogen, carbon dioxide, and acetic acid. These bacteria can be found in environments like hot springs, compost piles, and oil wells. It's important to note that individual species within this genus may have additional specific characteristics or requirements for growth.

Succinate-semialdehyde dehydrogenase (SSDH) is an enzyme involved in the metabolism of the neurotransmitter gamma-aminobutyric acid (GABA). Specifically, SSDH catalyzes the conversion of succinic semialdehyde to succinate in the final step of the GABA degradation pathway. This enzyme plays a critical role in maintaining the balance of GABA levels in the brain and is therefore essential for normal neurological function. Deficiencies or mutations in SSDH can lead to neurological disorders, including developmental delays, intellectual disability, and seizures.

I'm sorry for any confusion, but "Hydrogen" is not a medical term. It is a chemical element with the symbol H and atomic number 1. It is the lightest and most abundant chemical element in the universe, making up about 75% of its elemental mass.

In a medical context, hydrogen can be discussed in terms of molecular hydrogen (H2) which has been studied for potential therapeutic benefits. Some research explores its use as an antioxidant and anti-inflammatory agent, but more studies are needed to confirm these effects and understand the mechanisms behind them.

Macromolecular substances, also known as macromolecules, are large, complex molecules made up of repeating subunits called monomers. These substances are formed through polymerization, a process in which many small molecules combine to form a larger one. Macromolecular substances can be naturally occurring, such as proteins, DNA, and carbohydrates, or synthetic, such as plastics and synthetic fibers.

In the context of medicine, macromolecular substances are often used in the development of drugs and medical devices. For example, some drugs are designed to bind to specific macromolecules in the body, such as proteins or DNA, in order to alter their function and produce a therapeutic effect. Additionally, macromolecular substances may be used in the creation of medical implants, such as artificial joints and heart valves, due to their strength and durability.

It is important for healthcare professionals to have an understanding of macromolecular substances and how they function in the body, as this knowledge can inform the development and use of medical treatments.

Phenanthrolines are a class of compounds that contain a phenanthrene core with two amine groups attached to adjacent carbon atoms. They are known for their ability to form complexes with metal ions and have been widely used in the field of medicinal chemistry as building blocks for pharmaceuticals, particularly in the development of antimalarial drugs such as chloroquine and quinine. Additionally, phenanthrolines have also been explored for their potential use in cancer therapy due to their ability to interfere with DNA replication and transcription. However, it's important to note that specific medical uses and applications of phenanthrolines will depend on the particular compound and its properties.

Butanes are a group of flammable, colorless gases that are often used as fuel or in the production of other chemicals. They have the chemical formula C4H10 and are composed of four carbon atoms and ten hydrogen atoms. Butanes are commonly found in natural gas and crude oil, and they can be extracted through a process called distillation.

There are two main types of butane: n-butane and isobutane. N-butane has a straight chain of four carbon atoms, while isobutane has a branched chain with one carbon atom branching off the main chain. Both forms of butane are used as fuel for lighters, stoves, and torches, and they are also used as refrigerants and in the production of aerosols.

Butanes are highly flammable and can be dangerous if not handled properly. They should be stored in a cool, well-ventilated area away from sources of ignition, and they should never be used near an open flame or other source of heat. Ingesting or inhaling butane can be harmful and can cause symptoms such as dizziness, nausea, and vomiting. If you suspect that you have been exposed to butane, it is important to seek medical attention immediately.

Mitochondria are specialized structures located inside cells that convert the energy from food into ATP (adenosine triphosphate), which is the primary form of energy used by cells. They are often referred to as the "powerhouses" of the cell because they generate most of the cell's supply of chemical energy. Mitochondria are also involved in various other cellular processes, such as signaling, differentiation, and apoptosis (programmed cell death).

Mitochondria have their own DNA, known as mitochondrial DNA (mtDNA), which is inherited maternally. This means that mtDNA is passed down from the mother to her offspring through the egg cells. Mitochondrial dysfunction has been linked to a variety of diseases and conditions, including neurodegenerative disorders, diabetes, and aging.

Formic acid esters are chemical compounds formed by the reaction between formic acid and alcohols. This reaction, known as esterification, results in the formation of an ester group where the hydroxyl group (-OH) of the alcohol was. The general formula for a formic acid ester is:

R-O-CO-CHO

Where R represents the alkyl or aromatic group derived from the alcohol.

Formic acid esters are used in various applications, including as solvents, flavorings, and fragrances. Some examples of formic acid esters include methyl formate (methyl methanoate), ethyl formate (ethyl methanoate), and propyl formate (propyl methanoate).

In a medical context, formic acid esters have been studied for their potential therapeutic uses. For instance, sodium formate has been used as a treatment for methanol poisoning, as it helps to metabolize the toxic alcohol and reduce its harmful effects on the body. However, formic acid esters are not commonly used in mainstream medical treatments or therapies.

Enzyme induction is a process by which the activity or expression of an enzyme is increased in response to some stimulus, such as a drug, hormone, or other environmental factor. This can occur through several mechanisms, including increasing the transcription of the enzyme's gene, stabilizing the mRNA that encodes the enzyme, or increasing the translation of the mRNA into protein.

In some cases, enzyme induction can be a beneficial process, such as when it helps the body to metabolize and clear drugs more quickly. However, in other cases, enzyme induction can have negative consequences, such as when it leads to the increased metabolism of important endogenous compounds or the activation of harmful procarcinogens.

Enzyme induction is an important concept in pharmacology and toxicology, as it can affect the efficacy and safety of drugs and other xenobiotics. It is also relevant to the study of drug interactions, as the induction of one enzyme by a drug can lead to altered metabolism and effects of another drug that is metabolized by the same enzyme.

Gel chromatography is a type of liquid chromatography that separates molecules based on their size or molecular weight. It uses a stationary phase that consists of a gel matrix made up of cross-linked polymers, such as dextran, agarose, or polyacrylamide. The gel matrix contains pores of various sizes, which allow smaller molecules to penetrate deeper into the matrix while larger molecules are excluded.

In gel chromatography, a mixture of molecules is loaded onto the top of the gel column and eluted with a solvent that moves down the column by gravity or pressure. As the sample components move down the column, they interact with the gel matrix and get separated based on their size. Smaller molecules can enter the pores of the gel and take longer to elute, while larger molecules are excluded from the pores and elute more quickly.

Gel chromatography is commonly used to separate and purify proteins, nucleic acids, and other biomolecules based on their size and molecular weight. It is also used in the analysis of polymers, colloids, and other materials with a wide range of applications in chemistry, biology, and medicine.

Glucose is a simple monosaccharide (or single sugar) that serves as the primary source of energy for living organisms. It's a fundamental molecule in biology, often referred to as "dextrose" or "grape sugar." Glucose has the molecular formula C6H12O6 and is vital to the functioning of cells, especially those in the brain and nervous system.

In the body, glucose is derived from the digestion of carbohydrates in food, and it's transported around the body via the bloodstream to cells where it can be used for energy. Cells convert glucose into a usable form through a process called cellular respiration, which involves a series of metabolic reactions that generate adenosine triphosphate (ATP)—the main currency of energy in cells.

Glucose is also stored in the liver and muscles as glycogen, a polysaccharide (multiple sugar) that can be broken down back into glucose when needed for energy between meals or during physical activity. Maintaining appropriate blood glucose levels is crucial for overall health, and imbalances can lead to conditions such as diabetes mellitus.

A multigene family is a group of genetically related genes that share a common ancestry and have similar sequences or structures. These genes are arranged in clusters on a chromosome and often encode proteins with similar functions. They can arise through various mechanisms, including gene duplication, recombination, and transposition. Multigene families play crucial roles in many biological processes, such as development, immunity, and metabolism. Examples of multigene families include the globin genes involved in oxygen transport, the immune system's major histocompatibility complex (MHC) genes, and the cytochrome P450 genes associated with drug metabolism.

Acetates, in a medical context, most commonly refer to compounds that contain the acetate group, which is an functional group consisting of a carbon atom bonded to two hydrogen atoms and an oxygen atom (-COO-). An example of an acetate is sodium acetate (CH3COONa), which is a salt formed from acetic acid (CH3COOH) and is often used as a buffering agent in medical solutions.

Acetates can also refer to a group of medications that contain acetate as an active ingredient, such as magnesium acetate, which is used as a laxative, or calcium acetate, which is used to treat high levels of phosphate in the blood.

In addition, acetates can also refer to a process called acetylation, which is the addition of an acetyl group (-COCH3) to a molecule. This process can be important in the metabolism and regulation of various substances within the body.

A chemical model is a simplified representation or description of a chemical system, based on the laws of chemistry and physics. It is used to explain and predict the behavior of chemicals and chemical reactions. Chemical models can take many forms, including mathematical equations, diagrams, and computer simulations. They are often used in research, education, and industry to understand complex chemical processes and develop new products and technologies.

For example, a chemical model might be used to describe the way that atoms and molecules interact in a particular reaction, or to predict the properties of a new material. Chemical models can also be used to study the behavior of chemicals at the molecular level, such as how they bind to each other or how they are affected by changes in temperature or pressure.

It is important to note that chemical models are simplifications of reality and may not always accurately represent every aspect of a chemical system. They should be used with caution and validated against experimental data whenever possible.

Medical Definition of Vitamin A:

Vitamin A is a fat-soluble vitamin that is essential for normal vision, immune function, and cell growth. It is also an antioxidant that helps protect the body's cells from damage caused by free radicals. Vitamin A can be found in two main forms: preformed vitamin A, which is found in animal products such as dairy, fish, and meat, particularly liver; and provitamin A carotenoids, which are found in plant-based foods such as fruits, vegetables, and vegetable oils.

The most active form of vitamin A is retinoic acid, which plays a critical role in the development and maintenance of the heart, lungs, kidneys, and other organs. Vitamin A deficiency can lead to night blindness, dry skin, and increased susceptibility to infections. Chronic vitamin A toxicity can cause nausea, dizziness, headaches, coma, and even death.

Pseudomonadaceae is a family of Gram-negative, rod-shaped bacteria within the class Gammaproteobacteria. The name "Pseudomonadaceae" comes from the type genus Pseudomonas, which means "false unitform." This refers to the fact that these bacteria can appear similar to other rod-shaped bacteria but have distinct characteristics.

Members of this family are typically motile, aerobic organisms with a single polar flagellum or multiple lateral flagella. They are widely distributed in various environments, including soil, water, and as part of the normal microbiota of plants and animals. Some species can cause diseases in humans, such as Pseudomonas aeruginosa, which is an opportunistic pathogen known to cause severe infections in individuals with weakened immune systems, cystic fibrosis, or burn wounds.

Pseudomonadaceae bacteria are metabolically versatile and can utilize various organic compounds as carbon sources. They often produce pigments, such as pyocyanin and fluorescein, which contribute to their identification in laboratory settings. The family Pseudomonadaceae includes several genera, with Pseudomonas being the most well-known and clinically relevant.

Acetoin is a chemical compound that is produced as a metabolic byproduct in certain types of bacteria, including some species of streptococcus and lactobacillus. It is a colorless liquid with a sweet, buttery odor and is used as a flavoring agent in the food industry. In addition to its use as a flavoring, acetoin has been studied for its potential antibacterial properties and its possible role in the development of biofilms. However, more research is needed to fully understand the potential uses and implications of this compound.

1-Butanol, also known as n-butanol or butyl alcohol, is a primary alcohol with a chemical formula of C4H9OH. It is a colorless liquid that is used as a solvent and in the manufacture of other chemicals. 1-Butanol has a wide range of applications including use as a paint thinner, in the production of rubber, and as a fuel additive. It is also found naturally in some foods and beverages.

In medical terms, 1-butanol may be used as an ingredient in topical medications or as a solvent for various pharmaceutical preparations. However, it is not typically used as a therapeutic agent on its own. Exposure to high levels of 1-butanol can cause irritation to the eyes, skin, and respiratory tract, and prolonged exposure may lead to more serious health effects.

Lactobacillus brevis is a species of gram-positive, rod-shaped, facultatively anaerobic bacteria that belongs to the lactic acid bacteria group. It is commonly found in various environments such as plants, soil, and fermented foods like sauerkraut, pickles, and sourdough bread. Lactobacillus brevis is also part of the normal microbiota of the human gastrointestinal tract and vagina.

This bacterium is known for its ability to produce lactic acid as a metabolic end-product, which contributes to the preservation and fermentation of food. Lactobacillus brevis can also produce other compounds with potential health benefits, such as bacteriocins, which have antibacterial properties against certain pathogenic bacteria.

In some cases, Lactobacillus brevis has been investigated for its probiotic potential, although more research is needed to fully understand its effects on human health. It's important to note that while some strains of Lactobacillus brevis may have beneficial properties, others can cause infections in individuals with weakened immune systems or underlying medical conditions.

Xylitol is a type of sugar alcohol used as a sugar substitute in various food and dental products. It has a sweet taste similar to sugar but with fewer calories and less impact on blood sugar levels, making it a popular choice for people with diabetes or those looking to reduce their sugar intake. Xylitol is also known to have dental benefits, as it can help prevent tooth decay by reducing the amount of bacteria in the mouth that cause cavities.

Medically speaking, xylitol is classified as a carbohydrate and has a chemical formula of C5H12O5. It occurs naturally in some fruits and vegetables, but most commercial xylitol is produced from corn cobs or other plant materials through a process called hydrogenation. While generally considered safe for human consumption, it can have a laxative effect in large amounts and may be harmful to dogs, so it's important to keep it out of reach of pets.

'Clostridium' is a genus of gram-positive, rod-shaped bacteria that are widely distributed in nature, including in soil, water, and the gastrointestinal tracts of animals and humans. Many species of Clostridium are anaerobic, meaning they can grow and reproduce in environments with little or no oxygen. Some species of Clostridium are capable of producing toxins that can cause serious and sometimes life-threatening illnesses in humans and animals.

Some notable species of Clostridium include:

* Clostridium tetani, which causes tetanus (also known as lockjaw)
* Clostridium botulinum, which produces botulinum toxin, the most potent neurotoxin known and the cause of botulism
* Clostridium difficile, which can cause severe diarrhea and colitis, particularly in people who have recently taken antibiotics
* Clostridium perfringens, which can cause food poisoning and gas gangrene.

It is important to note that not all species of Clostridium are harmful, and some are even beneficial, such as those used in the production of certain fermented foods like sauerkraut and natto. However, due to their ability to produce toxins and cause illness, it is important to handle and dispose of materials contaminated with Clostridium species carefully, especially in healthcare settings.

Cobalt is a chemical element with the symbol Co and atomic number 27. It is a hard, silver-white, lustrous, and brittle metal that is found naturally only in chemically combined form, except for small amounts found in meteorites. Cobalt is used primarily in the production of magnetic, wear-resistant, and high-strength alloys, as well as in the manufacture of batteries, magnets, and pigments.

In a medical context, cobalt is sometimes used in the form of cobalt-60, a radioactive isotope, for cancer treatment through radiation therapy. Cobalt-60 emits gamma rays that can be directed at tumors to destroy cancer cells. Additionally, small amounts of cobalt are present in some vitamin B12 supplements and fortified foods, as cobalt is an essential component of vitamin B12. However, exposure to high levels of cobalt can be harmful and may cause health effects such as allergic reactions, lung damage, heart problems, and neurological issues.

Cyclohexanols are a class of organic compounds that contain a cyclohexane ring (a six-carbon saturated ring) with a hydroxyl group (-OH) attached to it. The hydroxyl group makes these compounds alcohols, and the cyclohexane ring provides a unique structure that can adopt different conformations.

The presence of the hydroxyl group in cyclohexanols allows them to act as solvents, intermediates in chemical synthesis, and starting materials for the production of other chemicals. They are used in various industries, including pharmaceuticals, agrochemicals, and polymers.

Cyclohexanols can exist in different forms, such as cis- and trans-isomers, depending on the orientation of the hydroxyl group relative to the cyclohexane ring. The physical and chemical properties of these isomers can differ significantly due to their distinct structures and conformations.

Examples of cyclohexanols include cyclohexanol itself (C6H11OH), as well as its derivatives, such as methylcyclohexanol (C7H13OH) and phenylcyclohexanol (C12H15OH).

In a medical context, "hot temperature" is not a standard medical term with a specific definition. However, it is often used in relation to fever, which is a common symptom of illness. A fever is typically defined as a body temperature that is higher than normal, usually above 38°C (100.4°F) for adults and above 37.5-38°C (99.5-101.3°F) for children, depending on the source.

Therefore, when a medical professional talks about "hot temperature," they may be referring to a body temperature that is higher than normal due to fever or other causes. It's important to note that a high environmental temperature can also contribute to an elevated body temperature, so it's essential to consider both the body temperature and the environmental temperature when assessing a patient's condition.

Oxidoreductases acting on CH-CH group donors are a class of enzymes within the larger group of oxidoreductases, which are responsible for catalyzing oxidation-reduction reactions. Specifically, this subclass of enzymes acts upon donors containing a carbon-carbon (CH-CH) bond, where one atom or group of atoms is oxidized and another is reduced during the reaction process. These enzymes play crucial roles in various metabolic pathways, including the breakdown and synthesis of carbohydrates, lipids, and amino acids.

The reactions catalyzed by these enzymes involve the transfer of electrons and hydrogen atoms between the donor and an acceptor molecule. This process often results in the formation or cleavage of carbon-carbon bonds, making them essential for numerous biological processes. The systematic name for this class of enzymes is typically structured as "donor:acceptor oxidoreductase," where donor and acceptor represent the molecules involved in the electron transfer process.

Examples of enzymes that fall under this category include:

1. Aldehyde dehydrogenases (EC 1.2.1.3): These enzymes catalyze the oxidation of aldehydes to carboxylic acids, using NAD+ as an electron acceptor.
2. Dihydrodiol dehydrogenase (EC 1.3.1.14): This enzyme is responsible for the oxidation of dihydrodiols to catechols in the biodegradation of aromatic compounds.
3. Succinate dehydrogenase (EC 1.3.5.1): A key enzyme in the citric acid cycle, succinate dehydrogenase catalyzes the oxidation of succinate to fumarate and reduces FAD to FADH2.
4. Xylose reductase (EC 1.1.1.307): This enzyme is involved in the metabolism of pentoses, where it reduces xylose to xylitol using NADPH as a cofactor.

An apoenzyme is the protein component of an enzyme that is responsible for its catalytic activity. It combines with a cofactor, which can be either an organic or inorganic non-protein molecule, to form the active enzyme. The cofactor can be a metal ion or a small organic molecule called a coenzyme.

The term "apoenzyme" is used to describe the protein portion of an enzyme after it has lost its cofactor. When the apoenzyme combines with the cofactor, the active holoenzyme is formed, which is capable of carrying out the specific biochemical reaction for which the enzyme is responsible.

In some cases, the loss of a cofactor can result in the complete loss of enzymatic activity, while in other cases, the apoenzyme may retain some residual activity. The relationship between an apoenzyme and its cofactor is specific, meaning that each cofactor typically only binds to and activates one particular type of apoenzyme.

Toluene is not a medical condition or disease, but it is a chemical compound that is widely used in various industrial and commercial applications. Medically, toluene can be relevant as a substance of abuse due to its intoxicating effects when inhaled or sniffed. It is a colorless liquid with a distinctive sweet aroma, and it is a common solvent found in many products such as paint thinners, adhesives, and rubber cement.

In the context of medical toxicology, toluene exposure can lead to various health issues, including neurological damage, cognitive impairment, memory loss, nausea, vomiting, and hearing and vision problems. Chronic exposure to toluene can also cause significant harm to the developing fetus during pregnancy, leading to developmental delays, behavioral problems, and physical abnormalities.

According to the Diagnostic and Statistical Manual of Mental Disorders, Fifth Edition (DSM-5), alcohol-induced disorders are a category of mental disorders that are directly caused by substance/medication use. Specifically, alcohol-induced disorders refer to conditions where the primary cause is the use of alcohol or its withdrawal.

There are several types of alcohol-induced disorders, including:

1. Alcohol intoxication delirium: A state of confusion and disorientation that occurs due to excessive alcohol consumption.
2. Alcohol withdrawal delirium: A serious condition characterized by confusion, hallucinations, and tremors that can occur after a person stops drinking heavily and suddenly.
3. Alcohol-induced bipolar and related disorders: Mood disturbances that are directly caused by alcohol use or withdrawal.
4. Alcohol-induced depressive disorder: Depressive symptoms that are directly caused by alcohol use or withdrawal.
5. Alcohol-induced anxiety disorder: Anxiety symptoms that are directly caused by alcohol use or withdrawal.
6. Alcohol-induced sleep disorder: Sleep disturbances that are directly caused by alcohol use or withdrawal.
7. Alcohol-induced sexual dysfunction: Sexual problems that are directly caused by alcohol use or withdrawal.
8. Alcohol-induced major neurocognitive disorder: A severe decline in cognitive abilities, such as memory and decision-making skills, that is directly caused by alcohol use or withdrawal.

It's important to note that these disorders are distinct from alcohol use disorder (AUD), which refers to a pattern of problematic alcohol use that can lead to clinically significant impairment or distress. However, AUD can increase the risk of developing alcohol-induced disorders.

Prephenate Dehydrogenase (PDH) is an enzyme involved in the metabolic pathway known as the shikimate pathway, which is responsible for the biosynthesis of aromatic amino acids in plants, bacteria, and fungi. Specifically, PDH catalyzes the conversion of prephenate to 4-hydroxybenzoate, an important intermediate in the synthesis of various aromatic compounds.

The reaction catalyzed by Prephenate Dehydrogenase is a decarboxylative oxidation and involves the removal of two hydrogen atoms from the prephenate molecule, resulting in the formation of 4-hydroxybenzoate, carbon dioxide, and NADPH. The enzyme plays a crucial role in the biosynthesis of various natural products, including pigments, antibiotics, and other secondary metabolites.

There are several isoforms of Prephenate Dehydrogenase that have been identified, each with distinct properties and functions. The enzyme has been studied extensively as a potential target for the development of herbicides and antibiotics, due to its essential role in the metabolism of plants and bacteria.

Genotype, in genetics, refers to the complete heritable genetic makeup of an individual organism, including all of its genes. It is the set of instructions contained in an organism's DNA for the development and function of that organism. The genotype is the basis for an individual's inherited traits, and it can be contrasted with an individual's phenotype, which refers to the observable physical or biochemical characteristics of an organism that result from the expression of its genes in combination with environmental influences.

It is important to note that an individual's genotype is not necessarily identical to their genetic sequence. Some genes have multiple forms called alleles, and an individual may inherit different alleles for a given gene from each parent. The combination of alleles that an individual inherits for a particular gene is known as their genotype for that gene.

Understanding an individual's genotype can provide important information about their susceptibility to certain diseases, their response to drugs and other treatments, and their risk of passing on inherited genetic disorders to their offspring.

Genetic variation refers to the differences in DNA sequences among individuals and populations. These variations can result from mutations, genetic recombination, or gene flow between populations. Genetic variation is essential for evolution by providing the raw material upon which natural selection acts. It can occur within a single gene, between different genes, or at larger scales, such as differences in the number of chromosomes or entire sets of chromosomes. The study of genetic variation is crucial in understanding the genetic basis of diseases and traits, as well as the evolutionary history and relationships among species.

Acrolein is an unsaturated aldehyde with the chemical formula CH2CHCHO. It is a colorless liquid that has a distinct unpleasant odor and is highly reactive. Acrolein is produced by the partial oxidation of certain organic compounds, such as glycerol and fatty acids, and it is also found in small amounts in some foods, such as coffee and bread.

Acrolein is a potent irritant to the eyes, nose, and throat, and exposure to high levels can cause coughing, wheezing, and shortness of breath. It has been shown to have toxic effects on the lungs, heart, and nervous system, and prolonged exposure has been linked to an increased risk of cancer.

In the medical field, acrolein is sometimes used as a laboratory reagent or as a preservative for biological specimens. However, due to its potential health hazards, it must be handled with care and appropriate safety precautions should be taken when working with this compound.

Methylphenazonium methosulfate is not a medication itself, but rather a reagent used in the production and pharmacological research of certain medications. It's commonly used as a redox mediator, which means it helps to facilitate electron transfer in chemical reactions. In medical contexts, it may be used in the laboratory synthesis or testing of some drugs.

It's important to note that methylphenazonium methosulfate is not intended for direct medical use in humans or animals. Always consult with a healthcare professional or trusted medical source for information regarding specific medications and their uses.

"Geobacillus stearothermophilus" is a species of gram-positive, rod-shaped bacteria that is thermophilic, meaning it thrives at relatively high temperatures. It is commonly found in soil and hot springs, and can also be found in other environments such as compost piles, oil fields, and even in some food products.

The bacterium is known for its ability to form endospores that are highly resistant to heat, radiation, and chemicals, making it a useful organism for sterility testing and bioprotection applications. It has an optimum growth temperature of around 60-70°C (140-158°F) and can survive at temperatures up to 80°C (176°F).

In the medical field, "Geobacillus stearothermophilus" is not typically associated with human disease or infection. However, there have been rare cases of infections reported in immunocompromised individuals who have come into contact with contaminated medical devices or materials.

High-performance liquid chromatography (HPLC) is a type of chromatography that separates and analyzes compounds based on their interactions with a stationary phase and a mobile phase under high pressure. The mobile phase, which can be a gas or liquid, carries the sample mixture through a column containing the stationary phase.

In HPLC, the mobile phase is a liquid, and it is pumped through the column at high pressures (up to several hundred atmospheres) to achieve faster separation times and better resolution than other types of liquid chromatography. The stationary phase can be a solid or a liquid supported on a solid, and it interacts differently with each component in the sample mixture, causing them to separate as they travel through the column.

HPLC is widely used in analytical chemistry, pharmaceuticals, biotechnology, and other fields to separate, identify, and quantify compounds present in complex mixtures. It can be used to analyze a wide range of substances, including drugs, hormones, vitamins, pigments, flavors, and pollutants. HPLC is also used in the preparation of pure samples for further study or use.

"Drosophila" is a genus of small flies, also known as fruit flies. The most common species used in scientific research is "Drosophila melanogaster," which has been a valuable model organism for many areas of biological and medical research, including genetics, developmental biology, neurobiology, and aging.

The use of Drosophila as a model organism has led to numerous important discoveries in genetics and molecular biology, such as the identification of genes that are associated with human diseases like cancer, Parkinson's disease, and obesity. The short reproductive cycle, large number of offspring, and ease of genetic manipulation make Drosophila a powerful tool for studying complex biological processes.

'Alcaligenes' is a genus of gram-negative, aerobic bacteria that are commonly found in soil, water, and the respiratory and intestinal tracts of animals. These bacteria are capable of using a variety of organic compounds as their sole source of carbon and energy. Some species of Alcaligenes have been known to cause opportunistic infections in humans, particularly in individuals with weakened immune systems. However, they are not considered major human pathogens.

The name 'Alcaligenes' comes from the Latin word "alcali," meaning "alkali," and the Greek word "genos," meaning "kind" or "race." This is because many species of Alcaligenes can grow in alkaline environments with a pH above 7.

It's worth noting that while Alcaligenes species are not typically harmful to healthy individuals, they may be resistant to certain antibiotics and can cause serious infections in people with compromised immune systems. Therefore, it is important for healthcare professionals to consider the possibility of Alcaligenes infection in patients who are at risk and to choose appropriate antibiotic therapy based on laboratory testing.

Glycolysis is a fundamental metabolic pathway that occurs in the cytoplasm of cells, consisting of a series of biochemical reactions. It's the process by which a six-carbon glucose molecule is broken down into two three-carbon pyruvate molecules. This process generates a net gain of two ATP molecules (the main energy currency in cells), two NADH molecules, and two water molecules.

Glycolysis can be divided into two stages: the preparatory phase (or 'energy investment' phase) and the payoff phase (or 'energy generation' phase). During the preparatory phase, glucose is phosphorylated twice to form glucose-6-phosphate and then converted to fructose-1,6-bisphosphate. These reactions consume two ATP molecules but set up the subsequent breakdown of fructose-1,6-bisphosphate into triose phosphates in the payoff phase. In this second stage, each triose phosphate is further oxidized and degraded to produce one pyruvate molecule, one NADH molecule, and one ATP molecule through substrate-level phosphorylation.

Glycolysis does not require oxygen to proceed; thus, it can occur under both aerobic (with oxygen) and anaerobic (without oxygen) conditions. In the absence of oxygen, the pyruvate produced during glycolysis is further metabolized through fermentation pathways such as lactic acid fermentation or alcohol fermentation to regenerate NAD+, which is necessary for glycolysis to continue.

In summary, glycolysis is a crucial process in cellular energy metabolism, allowing cells to convert glucose into ATP and other essential molecules while also serving as a starting point for various other biochemical pathways.

An allele is a variant form of a gene that is located at a specific position on a specific chromosome. Alleles are alternative forms of the same gene that arise by mutation and are found at the same locus or position on homologous chromosomes.

Each person typically inherits two copies of each gene, one from each parent. If the two alleles are identical, a person is said to be homozygous for that trait. If the alleles are different, the person is heterozygous.

For example, the ABO blood group system has three alleles, A, B, and O, which determine a person's blood type. If a person inherits two A alleles, they will have type A blood; if they inherit one A and one B allele, they will have type AB blood; if they inherit two B alleles, they will have type B blood; and if they inherit two O alleles, they will have type O blood.

Alleles can also influence traits such as eye color, hair color, height, and other physical characteristics. Some alleles are dominant, meaning that only one copy of the allele is needed to express the trait, while others are recessive, meaning that two copies of the allele are needed to express the trait.

In the field of medicine, "time factors" refer to the duration of symptoms or time elapsed since the onset of a medical condition, which can have significant implications for diagnosis and treatment. Understanding time factors is crucial in determining the progression of a disease, evaluating the effectiveness of treatments, and making critical decisions regarding patient care.

For example, in stroke management, "time is brain," meaning that rapid intervention within a specific time frame (usually within 4.5 hours) is essential to administering tissue plasminogen activator (tPA), a clot-busting drug that can minimize brain damage and improve patient outcomes. Similarly, in trauma care, the "golden hour" concept emphasizes the importance of providing definitive care within the first 60 minutes after injury to increase survival rates and reduce morbidity.

Time factors also play a role in monitoring the progression of chronic conditions like diabetes or heart disease, where regular follow-ups and assessments help determine appropriate treatment adjustments and prevent complications. In infectious diseases, time factors are crucial for initiating antibiotic therapy and identifying potential outbreaks to control their spread.

Overall, "time factors" encompass the significance of recognizing and acting promptly in various medical scenarios to optimize patient outcomes and provide effective care.

Genetic transcription is the process by which the information in a strand of DNA is used to create a complementary RNA molecule. This process is the first step in gene expression, where the genetic code in DNA is converted into a form that can be used to produce proteins or functional RNAs.

During transcription, an enzyme called RNA polymerase binds to the DNA template strand and reads the sequence of nucleotide bases. As it moves along the template, it adds complementary RNA nucleotides to the growing RNA chain, creating a single-stranded RNA molecule that is complementary to the DNA template strand. Once transcription is complete, the RNA molecule may undergo further processing before it can be translated into protein or perform its functional role in the cell.

Transcription can be either "constitutive" or "regulated." Constitutive transcription occurs at a relatively constant rate and produces essential proteins that are required for basic cellular functions. Regulated transcription, on the other hand, is subject to control by various intracellular and extracellular signals, allowing cells to respond to changing environmental conditions or developmental cues.

In the context of medicine and health, "temperance" refers to moderation or self-restraint in the consumption of potentially harmful substances, particularly alcohol. It promotes a balanced lifestyle that avoids excessive habits, such as overeating, substance abuse, or any other activities that could negatively impact one's health.

However, it is important to note that "temperance" itself is not a medical term per se but has been used in various historical and social contexts related to health promotion and disease prevention.

Cyanamide is a chemical compound with the formula NH2CN. It is a colorless, crystalline solid that is highly soluble in water and has an ammonia-like odor. Cyanamide is used as a reagent in organic synthesis and as a fertilizer.

In a medical context, cyanamide may be used as a drug to treat certain conditions. For example, it has been used as a muscle relaxant and to reduce muscle spasms in people with multiple sclerosis. It is also being studied as a potential treatment for alcohol dependence, as it may help to reduce cravings and withdrawal symptoms.

It is important to note that cyanamide can be toxic in high doses, and it should only be used under the supervision of a healthcare professional.

Genetic polymorphism refers to the occurrence of multiple forms (called alleles) of a particular gene within a population. These variations in the DNA sequence do not generally affect the function or survival of the organism, but they can contribute to differences in traits among individuals. Genetic polymorphisms can be caused by single nucleotide changes (SNPs), insertions or deletions of DNA segments, or other types of genetic rearrangements. They are important for understanding genetic diversity and evolution, as well as for identifying genetic factors that may contribute to disease susceptibility in humans.

Phenylethyl Alcohol is not a medical term per se, but it is a chemical compound with the formula C8H10O. It is a colorless oily liquid that is used as a fragrance ingredient in cosmetics and personal care products due to its rose-like odor.

In a medical context, Phenylethyl Alcohol may be mentioned in relation to its potential antimicrobial properties or as a component of certain pharmaceutical preparations. However, it is not a medication or treatment on its own. It is important to note that while Phenylethyl Alcohol has been studied for its potential health benefits, more research is needed before any definitive conclusions can be drawn.

Site-directed mutagenesis is a molecular biology technique used to introduce specific and targeted changes to a specific DNA sequence. This process involves creating a new variant of a gene or a specific region of interest within a DNA molecule by introducing a planned, deliberate change, or mutation, at a predetermined site within the DNA sequence.

The methodology typically involves the use of molecular tools such as PCR (polymerase chain reaction), restriction enzymes, and/or ligases to introduce the desired mutation(s) into a plasmid or other vector containing the target DNA sequence. The resulting modified DNA molecule can then be used to transform host cells, allowing for the production of large quantities of the mutated gene or protein for further study.

Site-directed mutagenesis is a valuable tool in basic research, drug discovery, and biotechnology applications where specific changes to a DNA sequence are required to understand gene function, investigate protein structure/function relationships, or engineer novel biological properties into existing genes or proteins.

Aerobiosis is the process of living, growing, and functioning in the presence of oxygen. It refers to the metabolic processes that require oxygen to break down nutrients and produce energy in cells. This is in contrast to anaerobiosis, which is the ability to live and grow in the absence of oxygen.

In medical terms, aerobiosis is often used to describe the growth of microorganisms, such as bacteria and fungi, that require oxygen to survive and multiply. These organisms are called aerobic organisms, and they play an important role in many biological processes, including decomposition and waste breakdown.

However, some microorganisms are unable to grow in the presence of oxygen and are instead restricted to environments where oxygen is absent or limited. These organisms are called anaerobic organisms, and their growth and metabolism are referred to as anaerobiosis.

1-Pyrroline-5-Carboxylate Dehydrogenase (PCD) is an enzyme that catalyzes the chemical reaction involved in the metabolism of proline, an amino acid. The enzyme converts 1-pyrroline-5-carboxylate to glutamate semialdehyde, which is then further metabolized to glutamate. This reaction is important in the regulation of proline levels in cells and is also a part of the cell's stress response. A deficiency in PCD can lead to an accumulation of 1-pyrroline-5-carboxylate, which can cause neurological symptoms and other health problems.

X-ray crystallography is a technique used in structural biology to determine the three-dimensional arrangement of atoms in a crystal lattice. In this method, a beam of X-rays is directed at a crystal and diffracts, or spreads out, into a pattern of spots called reflections. The intensity and angle of each reflection are measured and used to create an electron density map, which reveals the position and type of atoms in the crystal. This information can be used to determine the molecular structure of a compound, including its shape, size, and chemical bonds. X-ray crystallography is a powerful tool for understanding the structure and function of biological macromolecules such as proteins and nucleic acids.

Alcoholic liver disease (ALD) is a term that encompasses a spectrum of liver disorders caused by excessive alcohol consumption. The three main stages of ALD are:

1. Fatty Liver: This is the earliest stage of ALD, characterized by the accumulation of fat droplets within liver cells (hepatocytes). It's often reversible with abstinence from alcohol.

2. Alcoholic Hepatitis: This is a more severe form of ALD, characterized by inflammation and damage to the liver cells. It can range from mild to severe, and severe cases can lead to liver failure. Symptoms may include jaundice, abdominal pain, and fever.

3. Cirrhosis: This is the most advanced stage of ALD, characterized by widespread scarring (fibrosis) and nodular transformation of the liver. It's irreversible and can lead to complications such as liver failure, portal hypertension, and increased risk of liver cancer.

The development and progression of ALD are influenced by various factors, including the amount and duration of alcohol consumption, genetic predisposition, nutritional status, and co-existing viral hepatitis or other liver diseases. Abstaining from alcohol is the most effective way to prevent and manage ALD.

Anaerobic bacteria are a type of bacteria that do not require oxygen to grow and survive. Instead, they can grow in environments that have little or no oxygen. Some anaerobic bacteria can even be harmed or killed by exposure to oxygen. These bacteria play important roles in many natural processes, such as decomposition and the breakdown of organic matter in the digestive system. However, some anaerobic bacteria can also cause disease in humans and animals, particularly when they infect areas of the body that are normally oxygen-rich. Examples of anaerobic bacterial infections include tetanus, gas gangrene, and dental abscesses.

Formaldehyde is a colorless, pungent, and volatile chemical compound with the formula CH2O. It is a naturally occurring substance that is found in certain fruits like apples and vegetables, as well as in animals. However, the majority of formaldehyde used in industry is synthetically produced.

In the medical field, formaldehyde is commonly used as a preservative for biological specimens such as organs, tissues, and cells. It works by killing bacteria and inhibiting the decaying process. Formaldehyde is also used in the production of various industrial products, including adhesives, resins, textiles, and paper products.

However, formaldehyde can be harmful to human health if inhaled or ingested in large quantities. It can cause irritation to the eyes, nose, throat, and skin, and prolonged exposure has been linked to respiratory problems and cancer. Therefore, it is essential to handle formaldehyde with care and use appropriate safety measures when working with this chemical compound.

Culture media is a substance that is used to support the growth of microorganisms or cells in an artificial environment, such as a petri dish or test tube. It typically contains nutrients and other factors that are necessary for the growth and survival of the organisms being cultured. There are many different types of culture media, each with its own specific formulation and intended use. Some common examples include blood agar, which is used to culture bacteria; Sabouraud dextrose agar, which is used to culture fungi; and Eagle's minimum essential medium, which is used to culture animal cells.

Octopodiformes is a taxonomic order that includes two main groups: octopuses (Octopoda) and vampire squids (Vampyroteuthis infernalis). This grouping is based on similarities in their fossil record and molecular data. Although they are commonly referred to as squids, vampire squids are not true squids, which belong to a different order called Teuthida.

Octopodiformes are characterized by several features, including:

1. A highly developed brain and complex nervous system.
2. Eight arms with suckers, but no tentacles.
3. The ability to change their skin color and texture for camouflage.
4. Three hearts that pump blood through their bodies.
5. Blue blood due to the copper-based protein hemocyanin.
6. A siphon used for jet propulsion and other functions, such as waste expulsion and mating.
7. Ink sacs for defense against predators.

Octopuses are known for their intelligence, problem-solving abilities, and short lifespans (usually less than two years). Vampire squids, on the other hand, live in deep ocean environments and have a unique feeding strategy that involves filtering organic matter from the water. They can also produce bioluminescent displays to confuse predators.

It is important to note that while Octopodiformes is a well-supported taxonomic group, there is still ongoing research and debate about the relationships among cephalopods (the class that includes octopuses, squids, cuttlefish, and nautiluses) and their classification.

Glutaryl-CoA Dehydrogenase (GCDH) is an enzyme that plays a crucial role in the catabolism of the amino acids lysine and hydroxylysine. It is located in the inner mitochondrial membrane and functions as a homotetramer, with each subunit containing one molecule of FAD as a cofactor.

GCDH catalyzes the oxidative decarboxylation of glutaryl-CoA to form succinyl-CoA, which is then further metabolized in the citric acid cycle. This reaction also involves the reduction of FAD to FADH2, which can subsequently be used in the electron transport chain to generate ATP.

Deficiency in GCDH function can lead to a rare inherited disorder called glutaric acidemia type I (GA-I), which is characterized by an accumulation of glutaryl-CoA and its metabolites, including glutaric acid and 3-hydroxyglutaric acid. These metabolites can cause neurological damage and intellectual disability if left untreated.

Enzymes are complex proteins that act as catalysts to speed up chemical reactions in the body. They help to lower activation energy required for reactions to occur, thereby enabling the reaction to happen faster and at lower temperatures. Enzymes work by binding to specific molecules, called substrates, and converting them into different molecules, called products. This process is known as catalysis.

Enzymes are highly specific and will only catalyze one particular reaction with a specific substrate. The shape of the enzyme's active site, where the substrate binds, determines this specificity. Enzymes can be regulated by various factors such as temperature, pH, and the presence of inhibitors or activators. They play a crucial role in many biological processes, including digestion, metabolism, and DNA replication.

I apologize for any confusion, but "plants" is not a term that has a medical definition. The term "plants" refers to a large and diverse group of organisms that obtain their energy through photosynthesis, which is the process of converting sunlight into chemical energy. Plants are typically characterized by having cells with cell walls containing cellulose, chloroplasts containing the pigment chlorophyll, and the ability to synthesize their own food through photosynthesis.

In a medical or biological context, you might be thinking of "plant-based" or "phytomedicine," which refer to the use of plants or plant extracts as a form of medicine or treatment. Phytomedicines have been used for thousands of years in many traditional systems of medicine, and some plant-derived compounds have been found to have therapeutic benefits in modern medicine as well. However, "plants" itself does not have a medical definition.

Dioctyl Sulfosuccinic Acid (DOS) is a type of organic compound that is used as a surfactant and a dispersing agent in various industrial and commercial applications. It is a white to off-white crystalline powder, soluble in water and most organic solvents.

In medical terms, Dioctyl Sulfosuccinic Acid is not commonly used as a therapeutic agent. However, it may be used as an excipient or a component of the formulation in some pharmaceutical products. It has been used as a component in some oral and topical medications to improve their solubility, absorption, and stability.

It is important to note that while Dioctyl Sulfosuccinic Acid itself is not considered harmful, like any other chemical substance, it should be handled with care and used appropriately to avoid any potential health risks.

Alcohol withdrawal delirium, also known as delirium tremens (DTs), is a serious and potentially life-threatening complication that can occur in people who are dependent on alcohol and suddenly stop or significantly reduce their consumption. It is a form of alcohol withdrawal syndrome that is characterized by the sudden onset of severe confusion, agitation, hallucinations, tremors, and autonomic hyperactivity.

The diagnostic criteria for alcohol withdrawal delirium, as outlined in the Diagnostic and Statistical Manual of Mental Disorders (DSM-5), include:

1. Disturbance in consciousness (i.e., reduced clarity of awareness of the environment) with reduced ability to focus, sustain, or shift attention.
2. A change in cognition (such as memory deficit, disorientation, or language disturbance) or the development of a perceptual disturbance that is not better explained by another medical condition or substance use disorder.
3. The disturbance develops over a short period of time (usually hours to a few days) and tends to fluctuate throughout the day.
4. There is evidence from the history, physical examination, or laboratory findings that the symptoms are caused by alcohol withdrawal.
5. The symptoms cannot be better explained by another medical condition, medication use, or substance intoxication or withdrawal.

Alcohol withdrawal delirium is a medical emergency and requires immediate treatment in a hospital setting. Treatment typically involves the use of medications to manage symptoms, such as benzodiazepines to reduce agitation and prevent seizures, and antipsychotic medications to treat hallucinations and delusions. Supportive care, such as fluid and electrolyte replacement, may also be necessary to prevent dehydration and other complications.

Oxidoreductases acting on CH-NH group donors are a class of enzymes within the larger group of oxidoreductases, which are responsible for catalyzing oxidation-reduction reactions. Specifically, this subclass of enzymes acts on CH-NH group donors, where the CH-NH group is a chemical functional group consisting of a carbon atom (C) bonded to a nitrogen atom (N) via a single covalent bond.

These enzymes play a crucial role in various biological processes by transferring electrons from the CH-NH group donor to an acceptor molecule, which results in the oxidation of the donor and reduction of the acceptor. This process can lead to the formation or breakdown of chemical bonds, and plays a key role in metabolic pathways such as amino acid degradation and nitrogen fixation.

Examples of enzymes that fall within this class include:

* Amino oxidases, which catalyze the oxidative deamination of amino acids to produce alpha-keto acids, ammonia, and hydrogen peroxide.
* Transaminases, which transfer an amino group from one molecule to another, often in the process of amino acid biosynthesis or degradation.
* Amine oxidoreductases, which catalyze the oxidation of primary amines to aldehydes and secondary amines to ketones, with the concomitant reduction of molecular oxygen to hydrogen peroxide.

DNA Sequence Analysis is the systematic determination of the order of nucleotides in a DNA molecule. It is a critical component of modern molecular biology, genetics, and genetic engineering. The process involves determining the exact order of the four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - in a DNA molecule or fragment. This information is used in various applications such as identifying gene mutations, studying evolutionary relationships, developing molecular markers for breeding, and diagnosing genetic diseases.

The process of DNA Sequence Analysis typically involves several steps, including DNA extraction, PCR amplification (if necessary), purification, sequencing reaction, and electrophoresis. The resulting data is then analyzed using specialized software to determine the exact sequence of nucleotides.

In recent years, high-throughput DNA sequencing technologies have revolutionized the field of genomics, enabling the rapid and cost-effective sequencing of entire genomes. This has led to an explosion of genomic data and new insights into the genetic basis of many diseases and traits.

20-α-Hydroxysteroid Dehydrogenase (20-α-HSD) is an enzyme that catalyzes the conversion of steroids, specifically the oxidation of 20α-hydroxysteroids to 20-keto steroids. This enzyme plays a crucial role in the metabolism and regulation of steroid hormones, such as corticosteroids and progestogens.

In the adrenal gland, 20-α-HSD is involved in the biosynthesis and interconversion of various corticosteroids, including cortisol, cortisone, and aldosterone. By catalyzing the conversion of cortisol to cortisone or vice versa, this enzyme helps maintain a balance between active and inactive forms of these hormones, which is essential for proper physiological functioning.

In the reproductive system, 20-α-HSD is involved in the metabolism of progestogens, such as progesterone and its derivatives. This enzyme can convert active forms of progestogens into their inactive counterparts, thereby regulating their levels and activity within the body.

Dysregulation or mutations in 20-α-HSD have been implicated in several medical conditions, including adrenal insufficiency, congenital adrenal hyperplasia, and certain reproductive disorders.

Alpha-ketoglutaric acid, also known as 2-oxoglutarate, is not an acid in the traditional sense but is instead a key molecule in the Krebs cycle (citric acid cycle), which is a central metabolic pathway involved in cellular respiration. Alpha-ketoglutaric acid is a crucial intermediate in the process of converting carbohydrates, fats, and proteins into energy through oxidation. It plays a vital role in amino acid synthesis and the breakdown of certain amino acids. Additionally, it serves as an essential cofactor for various enzymes involved in numerous biochemical reactions within the body. Any medical conditions or disorders related to alpha-ketoglutaric acid would typically be linked to metabolic dysfunctions or genetic defects affecting the Krebs cycle.

A Structure-Activity Relationship (SAR) in the context of medicinal chemistry and pharmacology refers to the relationship between the chemical structure of a drug or molecule and its biological activity or effect on a target protein, cell, or organism. SAR studies aim to identify patterns and correlations between structural features of a compound and its ability to interact with a specific biological target, leading to a desired therapeutic response or undesired side effects.

By analyzing the SAR, researchers can optimize the chemical structure of lead compounds to enhance their potency, selectivity, safety, and pharmacokinetic properties, ultimately guiding the design and development of novel drugs with improved efficacy and reduced toxicity.

Molecular structure, in the context of biochemistry and molecular biology, refers to the arrangement and organization of atoms and chemical bonds within a molecule. It describes the three-dimensional layout of the constituent elements, including their spatial relationships, bond lengths, and angles. Understanding molecular structure is crucial for elucidating the functions and reactivities of biological macromolecules such as proteins, nucleic acids, lipids, and carbohydrates. Various experimental techniques, like X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and cryo-electron microscopy (cryo-EM), are employed to determine molecular structures at atomic resolution, providing valuable insights into their biological roles and potential therapeutic targets.

Digitoxigenin is a steroidal compound that is derived from digitalis plants, such as Digitalis lanata and Digitalis purpurea. It is a genin, which means it is a type of cardiac glycoside that does not contain a sugar molecule. Digitoxigenin itself does not have any intrinsic biological activity, but it can be converted into other compounds that do have therapeutic effects.

Digitoxigenin is a key intermediate in the synthesis of several important drugs, including digoxin and digitoxin. These drugs are used to treat various heart conditions, such as congestive heart failure and atrial fibrillation, by increasing the force of heart contractions and slowing the heart rate.

It is worth noting that digitoxigenin and its derivatives can have toxic effects if used inappropriately or in excessive amounts. Therefore, they should only be administered under the close supervision of a qualified healthcare professional.

Complementary DNA (cDNA) is a type of DNA that is synthesized from a single-stranded RNA molecule through the process of reverse transcription. In this process, the enzyme reverse transcriptase uses an RNA molecule as a template to synthesize a complementary DNA strand. The resulting cDNA is therefore complementary to the original RNA molecule and is a copy of its coding sequence, but it does not contain non-coding regions such as introns that are present in genomic DNA.

Complementary DNA is often used in molecular biology research to study gene expression, protein function, and other genetic phenomena. For example, cDNA can be used to create cDNA libraries, which are collections of cloned cDNA fragments that represent the expressed genes in a particular cell type or tissue. These libraries can then be screened for specific genes or gene products of interest. Additionally, cDNA can be used to produce recombinant proteins in heterologous expression systems, allowing researchers to study the structure and function of proteins that may be difficult to express or purify from their native sources.

Glyoxylates are organic compounds that are intermediates in various metabolic pathways, including the glyoxylate cycle. The glyoxylate cycle is a modified version of the Krebs cycle (also known as the citric acid cycle) and is found in plants, bacteria, and some fungi.

Glyoxylates are formed from the breakdown of certain amino acids or from the oxidation of one-carbon units. They can be converted into glycine, an important amino acid involved in various metabolic processes. In the glyoxylate cycle, glyoxylates are combined with acetyl-CoA to form malate and succinate, which can then be used to synthesize glucose or other organic compounds.

Abnormal accumulation of glyoxylates in the body can lead to the formation of calcium oxalate crystals, which can cause kidney stones and other health problems. Certain genetic disorders, such as primary hyperoxaluria, can result in overproduction of glyoxylates and increased risk of kidney stone formation.

DNA primers are short single-stranded DNA molecules that serve as a starting point for DNA synthesis. They are typically used in laboratory techniques such as the polymerase chain reaction (PCR) and DNA sequencing. The primer binds to a complementary sequence on the DNA template through base pairing, providing a free 3'-hydroxyl group for the DNA polymerase enzyme to add nucleotides and synthesize a new strand of DNA. This allows for specific and targeted amplification or analysis of a particular region of interest within a larger DNA molecule.

Medical Definition:

"Risk factors" are any attribute, characteristic or exposure of an individual that increases the likelihood of developing a disease or injury. They can be divided into modifiable and non-modifiable risk factors. Modifiable risk factors are those that can be changed through lifestyle choices or medical treatment, while non-modifiable risk factors are inherent traits such as age, gender, or genetic predisposition. Examples of modifiable risk factors include smoking, alcohol consumption, physical inactivity, and unhealthy diet, while non-modifiable risk factors include age, sex, and family history. It is important to note that having a risk factor does not guarantee that a person will develop the disease, but rather indicates an increased susceptibility.

Cinnamates are organic compounds that are derived from cinnamic acid. They contain a carbon ring with a double bond and a carboxylic acid group, making them aromatic acids. Cinnamates are widely used in the perfume industry due to their pleasant odor, and they also have various applications in the pharmaceutical and chemical industries.

In a medical context, cinnamates may be used as topical medications for the treatment of skin conditions such as fungal infections or inflammation. For example, cinnamate esters such as cinoxacin and ciclopirox are commonly used as antifungal agents in creams, lotions, and shampoos. These compounds work by disrupting the cell membranes of fungi, leading to their death.

Cinnamates may also have potential therapeutic benefits for other medical conditions. For instance, some studies suggest that cinnamate derivatives may have anti-inflammatory, antioxidant, and neuroprotective properties, making them promising candidates for the development of new drugs to treat diseases such as Alzheimer's and Parkinson's. However, more research is needed to confirm these effects and determine their safety and efficacy in humans.

'2,2'-Dipyridyl is an organic compound with the formula (C5H4N)2. It is a bidentate chelating ligand, which means that it can form stable coordination complexes with many metal ions by donating both of its nitrogen atoms to the metal. This ability to form complexes makes '2,2'-Dipyridyl useful in various applications, including as a catalyst in chemical reactions and as a reagent in the analysis of metal ions.

The compound is a solid at room temperature and has a molecular weight of 108.13 g/mol. It is soluble in organic solvents such as ethanol, acetone, and dichloromethane, but is insoluble in water. '2,2'-Dipyridyl is synthesized by the reaction of pyridine with formaldehyde and hydrochloric acid.

In medical contexts, '2,2'-Dipyridyl may be used as a reagent in diagnostic tests to detect the presence of certain metal ions in biological samples. However, it is not itself a drug or therapeutic agent.

Trifluoroethanol (TFE) is not a medical term, but it is a chemical compound with the formula CF3CH2OH. It is a colorless liquid that is used in various scientific and industrial applications. In the context of medical research, TFE has been used as a solvent for spectroscopic studies and as a reagent in organic synthesis.

TFE is known to have strong hydrogen bonding properties due to the electronegativity of the fluorine atoms, which makes it an excellent polar solvent. It can dissolve a wide range of organic compounds, including proteins and nucleic acids, making it useful for studying their structures and interactions.

While TFE is not used as a medication or therapeutic agent, it may have potential applications in medical research and drug development. For example, some studies have investigated the use of TFE as a cryoprotectant to prevent damage to cells and tissues during freezing and thawing. However, more research is needed to fully understand the potential benefits and risks of using TFE in medical contexts.

Amino acids are organic compounds that serve as the building blocks of proteins. They consist of a central carbon atom, also known as the alpha carbon, which is bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a variable side chain (R group). The R group can be composed of various combinations of atoms such as hydrogen, oxygen, sulfur, nitrogen, and carbon, which determine the unique properties of each amino acid.

There are 20 standard amino acids that are encoded by the genetic code and incorporated into proteins during translation. These include:

1. Alanine (Ala)
2. Arginine (Arg)
3. Asparagine (Asn)
4. Aspartic acid (Asp)
5. Cysteine (Cys)
6. Glutamine (Gln)
7. Glutamic acid (Glu)
8. Glycine (Gly)
9. Histidine (His)
10. Isoleucine (Ile)
11. Leucine (Leu)
12. Lysine (Lys)
13. Methionine (Met)
14. Phenylalanine (Phe)
15. Proline (Pro)
16. Serine (Ser)
17. Threonine (Thr)
18. Tryptophan (Trp)
19. Tyrosine (Tyr)
20. Valine (Val)

Additionally, there are several non-standard or modified amino acids that can be incorporated into proteins through post-translational modifications, such as hydroxylation, methylation, and phosphorylation. These modifications expand the functional diversity of proteins and play crucial roles in various cellular processes.

Amino acids are essential for numerous biological functions, including protein synthesis, enzyme catalysis, neurotransmitter production, energy metabolism, and immune response regulation. Some amino acids can be synthesized by the human body (non-essential), while others must be obtained through dietary sources (essential).

Saccharopine dehydrogenases are enzymes involved in the metabolism of the amino acid lysine. These enzymes catalyze the conversion of saccharopine, an intermediate compound in the lysine degradation pathway, into α-aminoadipic semialdehyde and glutamate. Saccharopine dehydrogenases play a crucial role in maintaining the balance of amino acids in the body and are found in various organisms, including bacteria, plants, and animals. In humans, mutations in the gene encoding one form of saccharopine dehydrogenase (Lysine Ketoglutarate Reductase/Saccharopine Dehydrogenase) have been associated with a rare genetic disorder called saccharopinuria, which is characterized by elevated levels of saccharopine in the urine and neurological symptoms.

Galactose dehydrogenases (GDH) are a group of enzymes that play a role in the metabolism of galactose, a simple sugar that is a component of lactose and other complex carbohydrates. These enzymes catalyze the oxidation of galactose to galactonate, using NAD+ as an electron acceptor. This reaction is part of the pathway that converts galactose to glucose in the body.

There are several different isoforms of galactose dehydrogenases found in various tissues and organisms, including:

1. GDH1 (also known as GALT): This is the primary form of galactose dehydrogenase found in humans and other mammals. It is located in the cytosol of cells and is responsible for the majority of galactose metabolism. Mutations in this gene can lead to a genetic disorder called classic galactosemia, which is characterized by an inability to metabolize galactose properly.
2. GDH2 (also known as G Aldo): This form of galactose dehydrogenase is found in the endoplasmic reticulum and is involved in the quality control of glycoproteins. It catalyzes the reverse reaction, reducing galactonate to galactose.
3. GDH3 (also known as G AldoX): This form of galactose dehydrogenase is found in the mitochondria and is involved in the metabolism of ascorbic acid (vitamin C). It also catalyzes the reverse reaction, reducing galactonate to galactose.
4. BGDH: This form of galactose dehydrogenase is found in bacteria and some plants. It is involved in the metabolism of both galactose and glucose.

Deficiencies or mutations in these enzymes can lead to various metabolic disorders, including galactosemia, which can cause a range of symptoms such as cataracts, developmental delays, and liver damage.

Gene expression is the process by which the information encoded in a gene is used to synthesize a functional gene product, such as a protein or RNA molecule. This process involves several steps: transcription, RNA processing, and translation. During transcription, the genetic information in DNA is copied into a complementary RNA molecule, known as messenger RNA (mRNA). The mRNA then undergoes RNA processing, which includes adding a cap and tail to the mRNA and splicing out non-coding regions called introns. The resulting mature mRNA is then translated into a protein on ribosomes in the cytoplasm through the process of translation.

The regulation of gene expression is a complex and highly controlled process that allows cells to respond to changes in their environment, such as growth factors, hormones, and stress signals. This regulation can occur at various stages of gene expression, including transcriptional activation or repression, RNA processing, mRNA stability, and translation. Dysregulation of gene expression has been implicated in many diseases, including cancer, genetic disorders, and neurological conditions.

Deoxyribonucleic acid (DNA) is the genetic material present in the cells of organisms where it is responsible for the storage and transmission of hereditary information. DNA is a long molecule that consists of two strands coiled together to form a double helix. Each strand is made up of a series of four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - that are linked together by phosphate and sugar groups. The sequence of these bases along the length of the molecule encodes genetic information, with A always pairing with T and C always pairing with G. This base-pairing allows for the replication and transcription of DNA, which are essential processes in the functioning and reproduction of all living organisms.

Binge drinking is a pattern of alcohol consumption that brings blood alcohol concentration (BAC) levels to 0.08 g/dL or above. For the typical adult, this corresponds to consuming 5 or more drinks (male), or 4 or more drinks (female), in about 2 hours.

It is a serious and dangerous form of alcohol consumption as it can lead to various negative health consequences such as injuries, violence, liver disease, heart disease, and sexually transmitted diseases, among others. Binge drinking is also associated with an increased risk of alcohol dependence.

Ribitol is a sugar alcohol, specifically a pentitol, that is a reduced form of the pentose sugar ribose. It is found in some fruits and vegetables, and it can also be produced synthetically. In biochemistry, ribitol plays a role as a component of certain coenzymes and as a constituent of the structural polysaccharides in the cell walls of some bacteria. It has been used in research and medical applications, such as in the study of bacterial metabolism and in the development of potential drugs.

Dihydrolipoyllysine-residue acetyltransferase is a type of enzyme that plays a crucial role in the cellular process of energy production, specifically in the citric acid cycle (also known as the Krebs cycle or tricarboxylic acid cycle). This enzyme is responsible for transferring an acetyl group from acetyl-CoA to a specific residue on another protein called dihydrolipoyl dehydrogenase.

The reaction catalyzed by this enzyme can be summarized as follows:
Acetyl-CoA + dihydrolipoyl dehydrogenase (E3-DHLA) -> CoA + acetylated-dihydrolipoyl dehydrogenase (E3-DHLAA)

The acetylation of the dihydrolipoyl dehydrogenase protein is a necessary step in the citric acid cycle, which helps generate energy in the form of ATP through a series of oxidation-reduction reactions. Defects or mutations in this enzyme can lead to various metabolic disorders and diseases.

Magnetic Resonance Spectroscopy (MRS) is a non-invasive diagnostic technique that provides information about the biochemical composition of tissues, including their metabolic state. It is often used in conjunction with Magnetic Resonance Imaging (MRI) to analyze various metabolites within body tissues, such as the brain, heart, liver, and muscles.

During MRS, a strong magnetic field, radio waves, and a computer are used to produce detailed images and data about the concentration of specific metabolites in the targeted tissue or organ. This technique can help detect abnormalities related to energy metabolism, neurotransmitter levels, pH balance, and other biochemical processes, which can be useful for diagnosing and monitoring various medical conditions, including cancer, neurological disorders, and metabolic diseases.

There are different types of MRS, such as Proton (^1^H) MRS, Phosphorus-31 (^31^P) MRS, and Carbon-13 (^13^C) MRS, each focusing on specific elements or metabolites within the body. The choice of MRS technique depends on the clinical question being addressed and the type of information needed for diagnosis or monitoring purposes.

Promoter regions in genetics refer to specific DNA sequences located near the transcription start site of a gene. They serve as binding sites for RNA polymerase and various transcription factors that regulate the initiation of gene transcription. These regulatory elements help control the rate of transcription and, therefore, the level of gene expression. Promoter regions can be composed of different types of sequences, such as the TATA box and CAAT box, and their organization and composition can vary between different genes and species.

I'm sorry for any confusion, but "Wisteria" is not a medical term. It is the name of a genus of flowering plants in the legume family, Fabaceae, that are native to Eastern Asia and North America. The plants are known for their long, hanging clusters of flowers in various colors including blue, purple, and white. They are often used as ornamental plants in gardens and parks. If you have any medical concerns or questions, I would be happy to try and help with those.

Biological evolution is the change in the genetic composition of populations of organisms over time, from one generation to the next. It is a process that results in descendants differing genetically from their ancestors. Biological evolution can be driven by several mechanisms, including natural selection, genetic drift, gene flow, and mutation. These processes can lead to changes in the frequency of alleles (variants of a gene) within populations, resulting in the development of new species and the extinction of others over long periods of time. Biological evolution provides a unifying explanation for the diversity of life on Earth and is supported by extensive evidence from many different fields of science, including genetics, paleontology, comparative anatomy, and biogeography.

Dimethylglycine dehydrogenase is an enzyme that plays a role in the metabolism of certain amino acids. The systematic name for this enzyme is N,N-dimethylglycine:electron transfer flavoprotein oxidoreductase. It catalyzes the following chemical reaction:

N,N-dimethylglycine + electron transfer flavoprotein → sarcosine + formaldehyde + reduced electron transfer flavoprotein

This enzyme is found in many organisms, including bacteria and humans. In humans, it is located in the mitochondria and is involved in the breakdown of the amino acid glycine. Mutations in the gene that encodes this enzyme can lead to a rare genetic disorder called dimethylglycine dehydrogenase deficiency, which is characterized by developmental delay, intellectual disability, and seizures.

Sorbitol is a type of sugar alcohol used as a sweetener in food and drinks, with about half the calories of table sugar. In a medical context, sorbitol is often used as a laxative to treat constipation, or as a sugar substitute for people with diabetes. It's also used as a bulk sweetener and humectant (a substance that helps retain moisture) in various pharmaceutical and cosmetic products.

When consumed in large amounts, sorbitol can have a laxative effect because it's not fully absorbed by the body and draws water into the intestines, which can lead to diarrhea. It's important for people with certain digestive disorders, such as irritable bowel syndrome or fructose intolerance, to avoid sorbitol and other sugar alcohols, as they can cause gastrointestinal symptoms like bloating, gas, and diarrhea.

Iodoacetic acid is not typically defined in the context of medical terminology, but rather it is a chemical compound with the formula CH2ICO2H. It is a colorless, oily liquid that is used in organic synthesis as an alkylating agent and also has been studied for its potential antibacterial and antifungal properties.

In medical contexts, iodoacetic acid may be mentioned in relation to its use in research or in the discussion of certain chemical reactions that may occur in the body. For example, it can inhibit the enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH), which plays a crucial role in energy metabolism. However, iodoacetic acid itself is not a medical treatment or therapy.

Aspartate-semialdehyde dehydrogenase (ASAD) is an enzyme that catalyzes the chemical reaction converting aspartate semialdehyde to beta-aspartyl-beta-AMP and then to beta-aspartate. This enzyme plays a crucial role in the biosynthesis of several amino acids, including lysine, threonine, and methionine. Defects in this enzyme can lead to serious genetic disorders, such as 3-methylcrotonyl-CoA carboxylase deficiency and Dwarfishism-deafness syndrome. The gene that encodes for ASAD is located on human chromosome 1 (1q21).

Enzyme activation refers to the process by which an enzyme becomes biologically active and capable of carrying out its specific chemical or biological reaction. This is often achieved through various post-translational modifications, such as proteolytic cleavage, phosphorylation, or addition of cofactors or prosthetic groups to the enzyme molecule. These modifications can change the conformation or structure of the enzyme, exposing or creating a binding site for the substrate and allowing the enzymatic reaction to occur.

For example, in the case of proteolytic cleavage, an inactive precursor enzyme, known as a zymogen, is cleaved into its active form by a specific protease. This is seen in enzymes such as trypsin and chymotrypsin, which are initially produced in the pancreas as inactive precursors called trypsinogen and chymotrypsinogen, respectively. Once they reach the small intestine, they are activated by enteropeptidase, a protease that cleaves a specific peptide bond, releasing the active enzyme.

Phosphorylation is another common mechanism of enzyme activation, where a phosphate group is added to a specific serine, threonine, or tyrosine residue on the enzyme by a protein kinase. This modification can alter the conformation of the enzyme and create a binding site for the substrate, allowing the enzymatic reaction to occur.

Enzyme activation is a crucial process in many biological pathways, as it allows for precise control over when and where specific reactions take place. It also provides a mechanism for regulating enzyme activity in response to various signals and stimuli, such as hormones, neurotransmitters, or changes in the intracellular environment.

Glycerol, also known as glycerine or glycerin, is a simple polyol (a sugar alcohol) with a sweet taste and a thick, syrupy consistency. It is a colorless, odorless, viscous liquid that is slightly soluble in water and freely miscible with ethanol and ether.

In the medical field, glycerol is often used as a medication or supplement. It can be used as a laxative to treat constipation, as a source of calories and energy for people who cannot eat by mouth, and as a way to prevent dehydration in people with certain medical conditions.

Glycerol is also used in the production of various medical products, such as medications, skin care products, and vaccines. It acts as a humectant, which means it helps to keep things moist, and it can also be used as a solvent or preservative.

In addition to its medical uses, glycerol is also widely used in the food industry as a sweetener, thickening agent, and moisture-retaining agent. It is generally recognized as safe (GRAS) by the U.S. Food and Drug Administration (FDA).

Metalloproteins are proteins that contain one or more metal ions as a cofactor, which is required for their biological activity. These metal ions play crucial roles in the catalytic function, structural stability, and electron transfer processes of metalloproteins. The types of metals involved can include iron, zinc, copper, magnesium, calcium, or manganese, among others. Examples of metalloproteins are hemoglobin (contains heme-bound iron), cytochrome c (contains heme-bound iron and functions in electron transfer), and carbonic anhydrase (contains zinc and catalyzes the conversion between carbon dioxide and bicarbonate).

Betaine-aldehyde dehydrogenase (BADH) is an enzyme involved in the metabolic pathway of betaine, a compound that helps protect cells from environmental stress and is important for maintaining cell volume and osmotic balance. The enzyme catalyzes the conversion of betaine aldehyde to betaine, using NAD+ as a cofactor.

Deficiency in BADH has been associated with certain genetic disorders, such as hyperbetalipoproteinemia type I, which is characterized by elevated levels of lipids and lipoproteins in the blood. Additionally, mutations in the BADH gene have been linked to an increased risk of alcoholism and alcohol-related disorders.

Amino alcohols are organic compounds containing both amine and hydroxyl (alcohol) functional groups. They have the general structure R-NH-OH, where R represents a carbon-containing group. Amino alcohols can be primary, secondary, or tertiary, depending on the number of alkyl or aryl groups attached to the nitrogen atom.

These compounds are important in many chemical and biological processes. For example, some amino alcohols serve as intermediates in the synthesis of pharmaceuticals, dyes, and polymers. In biochemistry, certain amino alcohols function as neurotransmitters or components of lipids.

Some common examples of amino alcohols include:

* Ethanolamine (monoethanolamine, MEA): a primary amino alcohol used in the production of detergents, emulsifiers, and pharmaceuticals
* Serinol: a primary amino alcohol that occurs naturally in some foods and is used as a flavoring agent
* Choline: a quaternary ammonium compound with a hydroxyl group, essential for human nutrition and found in various foods such as eggs, liver, and peanuts
* Trimethylamine (TMA): a tertiary amino alcohol that occurs naturally in some marine animals and is responsible for the "fishy" odor of their flesh.

I'm sorry for any confusion, but there seems to be a misunderstanding. Mathematics is not a medical term; it is a branch of science dedicated to the study of numbers, shapes, and structures. However, mathematics does have many applications in medicine, such as in modeling disease spread, analyzing medical images, or designing clinical trials. If you have any questions related to mathematics in a medical context, I'd be happy to help clarify those for you!

Alcohol dehydrogenases (ADH) (EC 1.1.1.1) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the ... In early 1960, the alcohol dehydrogenase (ADH) gene was discovered in fruit flies of the genus Drosophila melanogaster. Flies ... In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ... In humans, sequencing of the ADH1B gene (responsible for production of an alcohol dehydrogenase polypeptide) shows several ...
... a coniferyl-alcohol dehydrogenase (EC 1.1.1.194) is an enzyme that catalyzes the chemical reaction coniferyl alcohol + NADP+ ... Mansell RL, Babbel GR, Zenk MH (1976). "Multiple forms and specificity of coniferyl alcohol dehydrogenase from cambial regions ... "Purification and properties of isoenzymes of cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures". Eur. J. ... The systematic name of this enzyme class is coniferyl-alcohol:NADP+ oxidoreductase. This enzyme is also called CAD. ...
... (EC 1.1.99.36, NDMA-dependent alcohol dehydrogenase, nicotinoprotein alcohol ... Piersma SR, Visser AJ, de Vries S, Duine JA (March 1998). "Optical spectroscopy of nicotinoprotein alcohol dehydrogenase from ... Norin A, Piersma SR, Duine JA, Jörnvall H (May 2003). "Nicotinoprotein (NAD+ -containing) alcohol dehydrogenase: structural ... Schenkels P, Duine JA (April 2000). "Nicotinoprotein (NADH-containing) alcohol dehydrogenase from Rhodococcus erythropolis DSM ...
... (EC 1.1.5.5, type III ADH, membrane associated quinohaemoprotein alcohol dehydrogenase) is an ... "Quinoprotein alcohol dehydrogenase is involved in catabolic acetate production, while NAD-dependent alcohol dehydrogenase in ... "The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from ... Reactivity with ubiquinone of pyrroloquinoline quinone-dependent alcohol dehydrogenases purified from Acetobacter aceti and ...
Alcohol dehydrogenase may also refer to: Alcohol dehydrogenase (acceptor) Alcohol dehydrogenase (azurin) Alcohol dehydrogenase ... Alcohol dehydrogenase, iron containing 1 Alcohol dehydrogenase (NAD(P)+) Alcohol dehydrogenase (NADP+) Alcohol dehydrogenase ( ... Look up alcohol dehydrogenase in Wiktionary, the free dictionary. Alcohol dehydrogenases are enzymes that catalyze the ... Alcohol dehydrogenase (quinone) This disambiguation page lists articles associated with the title Alcohol dehydrogenase. If an ...
In enzymology, an allyl-alcohol dehydrogenase (EC 1.1.1.54) is an enzyme that catalyzes the chemical reaction allyl alcohol + ... Otsuka K (1958). "Triphosphopyridine nucleotide-allyl and -ethyl alcohol dehydrogenases from Escherichia coli". J. Gen. Appl. ... The systematic name of this enzyme class is allyl-alcohol:NADP+ oxidoreductase. ... NADP+ ⇌ {\displaystyle \rightleftharpoons } acrolein + NADPH + H+ Thus, the two substrates of this enzyme are allyl alcohol and ...
... a perillyl-alcohol dehydrogenase (EC 1.1.1.144) is an enzyme that catalyzes the chemical reaction perillyl alcohol + NAD+ ⇌ {\ ... This enzyme is also called perillyl alcohol dehydrogenase. This enzyme participates in limonene and pinene degradation. Ballal ... "Perillyl alcohol dehydrogenase from a soil pseudomonad". Biochem. Biophys. Res. Commun. 23 (4): 473-8. doi:10.1016/0006-291X(66 ... The systematic name of this enzyme class is perillyl-alcohol:NAD+ oxidoreductase. ...
... a cinnamyl-alcohol dehydrogenase (EC 1.1.1.195) is an enzyme that catalyzes the chemical reaction cinnamyl alcohol + NADP+ ⇌ {\ ... Sarni F, Grand C, Boudet AM (1984). "Purification and properties of cinnamoyl-CoA reductase and cinnamyl alcohol dehydrogenase ... Further studies on cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures". Eur. J. Biochem. 97 (2): 503-9. doi: ... Wyrambik D, Grisebach H (1975). "Purification and properties of isoenzymes of cinnamyl-alcohol dehydrogenase from soybean-cell- ...
... quinohemoprotein alcohol dehydrogenase, quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase, and alcohol:( ... Alcohol dehydrogenase Ameyama M; Adachi O (1982). Alcohol dehydrogenase from acetic acid bacteria, membrane-bound. Methods in ... an alcohol dehydrogenase (acceptor) (EC 1.1.99.8) is an enzyme that catalyzes the chemical reaction a primary alcohol + ... Purification and properties of the alcohol dehydrogenase of Pseudomonas sp. M27". Biochem. J. 104 (3): 953-9. doi:10.1042/ ...
... (EC 1.1.9.1, type II quinoprotein alcohol dehydrogenase, quinohaemoprotein ethanol dehydrogenase ... "Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory ... Groen BW, van Kleef MA, Duine JA (March 1986). "Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas testosteroni ... "Structure at 1.9 A resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5". Structure. 10 (6): 837- ...
Other names in common use include p-hydroxybenzyl alcohol dehydrogenase, benzyl alcohol dehydrogenase, and coniferyl alcohol ... an aryl-alcohol dehydrogenase (EC 1.1.1.90) is an enzyme that catalyzes the chemical reaction an aromatic alcohol + NAD+ ⇌ {\ ... "Identification and characterization of a nicotinamide adenine dinucleotide-dependent para-hydroxybenzyl alcohol-dehydrogenase ... Suhara K, Takemori S, Katagiri M (1969). "The purification and properties of benzylalcohol dehydrogenase from Pseudomonas sp". ...
Other names in common use include long-chain alcohol dehydrogenase, and fatty alcohol oxidoreductase. This enzyme participates ... a long-chain-alcohol dehydrogenase (EC 1.1.1.192) is an enzyme that catalyzes the chemical reaction a long-chain alcohol + 2 ... Lee T (April 1979). "Characterization of fatty alcohol:NAD+ oxidoreductase from rat liver". The Journal of Biological Chemistry ... The systematic name of this enzyme class is long-chain-alcohol:NAD+ oxidoreductase. ...
... a polyvinyl-alcohol dehydrogenase (acceptor) (EC 1.1.99.23) is an enzyme that catalyzes the chemical reaction polyvinyl alcohol ... Other names in common use include PVA dehydrogenase, and polyvinyl-alcohol:(acceptor) oxidoreductase. It employs one cofactor, ... pyrroloquinoline quinone-dependent polyvinyl alcohol dehydrogenase, in a bacterial symbiont, Pseudomonas sp. strain VM15C". ... the two substrates of this enzyme are polyvinyl alcohol and acceptor, whereas its two products are oxidized polyvinyl alcohol ...
... coniferyl alcohol dehydrogenase, NADPH-linked benzaldehyde reductase, and aryl-alcohol dehydrogenase (NADP+). Gross GG, Zenk MH ... an aryl-alcohol dehydrogenase (NADP+) (EC 1.1.1.91) is an enzyme that catalyzes the chemical reaction an aromatic alcohol + ... Other names in common use include aryl alcohol dehydrogenase (nicotinamide adenine dinucleotide, phosphate), ... 2. Purification and properties of aryl-alcohol: NADP-oxidoreductase from Neurospora crassa]". Eur. J. Biochem. (in German). 8 ( ...
Other names in common use include m-hydroxybenzyl alcohol dehydrogenase, m-hydroxybenzyl alcohol (NADP+) dehydrogenase, and m- ... a 3-hydroxybenzyl-alcohol dehydrogenase (EC 1.1.1.97) is an enzyme that catalyzes the chemical reaction 3-hydroxybenzyl alcohol ... Forrester PI, Gaucher GM (1972). "m-Hydroxybenzyl alcohol dehydrogenase from Penicillium urticae". Biochemistry. 11 (6): 1108- ... The systematic name of this enzyme class is 3-hydroxybenzyl-alcohol:NADP+ oxidoreductase. ...
... (EC 1.1.5.7, cyclic alcohol dehydrogenase, MCAD) is an enzyme with systematic name ... "Purification and characterization of membrane-bound quinoprotein cyclic alcohol dehydrogenase from Gluconobacter frateurii CHM ... Cyclic+alcohol+dehydrogenase+(quinone) at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ... This enzyme catalyses the following chemical reaction cyclic alcohol + quinone ⇌ {\displaystyle \rightleftharpoons } cyclic ...
... vinyl alcohol) dehydrogenase from Sphingomonas sp. strain 113P3, a novel-type quinohaemoprotein alcohol dehydrogenase". ... Polyvinyl alcohol dehydrogenase (cytochrome) (EC 1.1.2.6, PVA dehydrogenase, PVADH) is an enzyme with systematic name polyvinyl ... pyrroloquinoline quinone-dependent polyvinyl alcohol dehydrogenase, in a bacterial symbiont, Pseudomonas sp. strain VM15C". ... oxidized polyvinyl alcohol + ferrocytochrome c + H+ This enzyme participates in bacterial polyvinyl alcohol degradation. Shimao ...
... (EC 1.1.1.314) is an enzyme with systematic name germacra-1(10),4,11(13)-trien-12-ol:NADP+ ... Germacrene+A+alcohol+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC ... Demonstration of a cytochrome P450 (+)-germacrene a hydroxylase and NADP+-dependent sesquiterpenoid dehydrogenase(s) involved ...
... and alcohol dehydrogenase [NAD(P)]. This enzyme participates in glycolysis and gluconeogenesis. Alcohol dehydrogenase Fidge NH ... In enzymology, an alcohol dehydrogenase [NAD(P)+] (EC 1.1.1.71) is an enzyme that catalyzes the chemical reaction an alcohol + ... The systematic name of this enzyme class is alcohol:NAD(P)+ oxidoreductase. Other names in common use include retinal reductase ... NAD(P)+ ⇌ {\displaystyle \rightleftharpoons } an aldehyde + NAD(P)H + H+ The 3 substrates of this enzyme are alcohol, NAD+, and ...
... (EC 1.1.2.8, type I quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase ... "Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols". ... Alcohol+dehydrogenase+(cytochrome+c) at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ( ... Mennenga B, Kay CW, Görisch H (April 2009). "Quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: the unusual ...
... is a protein that in humans is encoded by the ADHFE1 gene. The ADHFE1 gene encodes ... "Entrez Gene: Alcohol dehydrogenase, iron containing 1". Retrieved 2017-06-16. Kardon T, Noël G, Vertommen D, Schaftingen EV ( ... "Alcohol dehydrogenase, iron containing, 1 promoter hypermethylation associated with colorectal cancer differentiation". BMC ... "Cloning and characterization of a novel human alcohol dehydrogenase gene (ADHFe1)". DNA Sequence. 13 (5): 301-6. doi:10.1080/ ...
S-nitrosoglutathione reductase (GSNOR) is a class III alcohol dehydrogenase (ADH) encoded by the ADH5 gene in humans. It is a ... More related to its alcohol dehydrogenase activity, GSNOR null mice show a 30% reduction in the LD50 for formaldehyde and a ... Jensen DE, Belka GK, Du Bois GC (April 1998). "S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III ... Staab CA, Alander J, Morgenstern R, Grafström RC, Höög JO (March 2009). "The Janus face of alcohol dehydrogenase 3". Chem. Biol ...
Salisbury SA, Forrest HS, Cruse WB, Kennard O (August 1979). "A novel coenzyme from bacterial primary alcohol dehydrogenases". ... The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group". The ... Methanol dehydrogenase (cytochrome c) (EC 1.1.2.7, methanol dehydrogenase, MDH) is an enzyme with systematic name methanol: ... 2 H+ A periplasmic quinoprotein alcohol dehydrogenase is only present in methylotrophic bacteria. Anthony C, Zatman LJ ( ...
In recognition of his contributions to the study of alcohol dehydrogenase Pettersson was invited to write a review on the topic ... In parallel with his study of alcohol dehydrogenase, Pettersson developed methods in enzyme kinetics based on mathematical ... Kvassman, J; Pettersson, G. (1976). "Kinetic transients in reduction of aldehydes catalysed by liver alcohol dehydrogenase". ... Pettersson, G.; Klinman, J. P. (1987). "Liver alcohol dehydrogenase". Crit. Rev. Biochem. 21 (4): 349-389. doi:10.3109/ ...
Glucose/ribitol dehydrogenase InterPro: IPR002347 Insect alcohol dehydrogenase family InterPro: IPR002424 2,3-dihydro-2,3- ... alcohol dehydrogenases. Most members of this family are proteins of about 250 to 300 amino acid residues. Most dehydrogenases ... As the first member of this family to be characterised was Drosophila alcohol dehydrogenase, this family used to be called ' ... Persson B, Krook M, Jornvall H (1991). "Characteristics of short-chain alcohol dehydrogenases and related enzymes". Eur. J. ...
Isopropanol dehydrogenase and alcohol dehydrogenase of Lactobacillus brevis var. hofuensis". Nippon Nogeikagaku Kaishi (in ... In enzymology, an isopropanol dehydrogenase (NADP+) (EC 1.1.1.80) is an enzyme that catalyzes the chemical reaction propan-2-ol ... This enzyme is also called isopropanol dehydrogenase (NADP+). This enzyme participates in propanoate metabolism. Hoshino K ( ...
"Overview of the role of alcohol dehydrogenase and aldehyde dehydrogenase and their variants in the genesis of alcohol-related ... "Alcohol Dehydrogenases, Aldehyde Dehydrogenases, and Alcohol Use Disorders: A Critical Review". Alcoholism: Clinical and ... ALDH18A1 Alcohol dehydrogenase PDB: 1o02​; Perez-Miller SJ, Hurley TD (June 2003). "Coenzyme isomerization is integral to ... "Alcohol and aldehyde dehydrogenase genotypes and alcoholism in Chinese men". American Journal of Human Genetics. 48 (4): 677-81 ...
acetaldehyde dehydrogenase alcohol dehydrogenase Delta12-fatty acid dehydrogenase glutamate dehydrogenase (an enzyme that can ... alpha-ketoglutarate dehydrogenase (uses NAD+) succinate dehydrogenase (uses FAD) malate dehydrogenase (uses NAD+) An IUPAC ... Goedde, HW; Agarwal, DP (1983). "Population genetic studies on aldehyde dehydrogenase isozyme deficiency and alcohol ... In the above case, the dehydrogenase has transferred a hydride while releasing a proton, H+, but dehydrogenases can also ...
Dyck LE (1995). "Polymorphism of a class 3 aldehyde dehydrogenase present in human saliva and in hair roots". Alcohol. Clin. ... Variable' and 'constant' enzymes within the alcohol and aldehyde dehydrogenase families". FEBS Lett. 283 (1): 85-8. doi:10.1016 ... "Structural features of stomach aldehyde dehydrogenase distinguish dimeric aldehyde dehydrogenase as a 'variable' enzyme. ' ... Aldehyde dehydrogenase, dimeric NADP-preferring is an enzyme that in humans is encoded by the ALDH3A1 gene. Aldehyde ...
ISBN 978-0716701743.[page needed] Raj SB, Ramaswamy S, Plapp BV (2014). "Yeast alcohol dehydrogenase structure and catalysis". ... NAD+ This reaction is catalyzed by alcohol dehydrogenase (ADH1 in baker's yeast). As shown by the reaction equation, glycolysis ... phenylethyl alcohol and gamma-butyrolactone, secondary products of alcoholic fermentation". Comptes Rendus de l'Académie des ... Ethanol contained in alcoholic beverages is produced by means of fermentation induced by yeast. Wine is produced by ...
Alcohol dehydrogenases (ADH) (EC 1.1.1.1) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the ... In early 1960, the alcohol dehydrogenase (ADH) gene was discovered in fruit flies of the genus Drosophila melanogaster. Flies ... In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ... In humans, sequencing of the ADH1B gene (responsible for production of an alcohol dehydrogenase polypeptide) shows several ...
Crystal structure of Alcohol dehydrogenase from Geobacillus stearothermophilus ... Characterization of the substrate scope of an alcohol dehydrogenase commonly used as methanol dehydrogenase.. Guo, X., Feng, Y. ... Many alcohol dehydrogenases (ADHs) catalyze oxidation of a broad scope of alcohols. When an NAD-dependent ADH oxidizes methanol ... Many alcohol dehydrogenases (ADHs) catalyze oxidation of a broad scope of alcohols. When an NAD-dependent ADH oxidizes methanol ...
Alcohol dehydrogenase E chain(4R)-2-METHYLPENTANE-2,4-DIOL2,3,4,5,6-PENTAFLUOROBENZYL ALCOHOLNICOTINAMIDE-ADENINE-DINUCLEOTIDE ... 6OWM: Horse liver F93W alcohol dehydrogenase complexed with NAD and pentafluorobenzyl alcohol. ...
Crystal structure of Alcohol dehydrogenase zinc-binding domain protein from Burkholderia ambifaria ... Alcohol dehydrogenase zinc-binding domain protein. A. 383. Burkholderia ambifaria MC40-6. Mutation(s): 0 Gene Names: BamMC406_ ... Crystal structure of Alcohol dehydrogenase zinc-binding domain protein from Burkholderia ambifaria. Abendroth, J., Mayclin, S.J ... Crystal structure of Alcohol dehydrogenase zinc-binding domain protein from Burkholderia ambifaria. *PDB DOI: https://doi.org/ ...
Protein target information for Aryl-alcohol dehydrogenase (Acinetobacter guillouiae). Find diseases associated with this ...
Inactive pseudoenzyme subunits in heterotetrameric BbsCD, a novel short-chain alcohol dehydrogenase involved in anaerobic ... Keywords: beta oxidation; pseudoenzyme; short-chain dehydrogenases/reductases; structural biology; toluene metabolism. ... succinyl-CoA dehydrogenase (BbsCD) from Thauera aromatica. BbsH, a member of the enoyl-CoA hydratase family, converts (E)- ... which belongs to the short-chain dehydrogenases/reductase (SDR) family. The BbsCD crystal structure shows a C2-symmetric ...
Synonyms: ADH-3, ADHX, Alcohol dehydrogenase 5, Alcohol dehydrogenase class chi chain, Alcohol dehydrogenase class-3, ... ... The alcohol dehydrogenase, class I (ADH2, ADH3) gene cluster can be linked to the alcohol dehydrogenase, class III gene (ADH5) ... Genetic variation in alcohol dehydrogenase and the beneficial effect of moderate alcohol consumption on myocardial infarction. ... Role of arginine 115 in fatty acid activation and formaldehyde dehydrogenase activity of human class III alcohol dehydrogenase. ...
Timeline for Family c.2.1.1: Alcohol dehydrogenase-like, C-terminal domain: *Family c.2.1.1: Alcohol dehydrogenase-like, C- ... Alcohol/glucose dehydrogenases, C-terminal domain. *Family c.2.1.1: Alcohol dehydrogenase-like, C-terminal domain appears in ... Putative zinc-binding alcohol dehydrogenase [102131] (1 species). *. Species Mouse (Mus musculus) [TaxId:10090] [102132] (1 PDB ... Cinnamyl alcohol dehydrogenase, ADH6 [110403] (1 species). *. Species Bakers yeast (Saccharomyces cerevisiae) [TaxId:4932] [ ...
All SLS cells were selectively deficient in the FALDH component of FAO, and had normal activity of fatty alcohol dehydrogenase ... Deficient activity of the fatty aldehyde dehydrogenase component of fatty alcohol:NAD+ oxidoreductase in cultured fibroblasts. ... and fatty alcohol dehydrogenase in cultured fibroblasts from seven unrelated SLS patients. ... is an inherited disorder associated with impaired fatty alcohol oxidation due to deficient activity of fatty alcohol:NAD+ ...
In this study, diversity of alcohol dehydrogenases in Lactobacillus species was investigated with a focus on L. reuteri. Nine ... the organism is likely to have alternative alcohol dehydrogenase(s) in the cytoplasm for transformation of the aldehyde. ... supporting the role of this bifuctional alcohol/aldehyde dehydrogenase in ethanol production. To the best of our knowledge, ...
Mechanistic studies on equine liver alcohol dehydrogenase. I. the stoichiometry relationship of the coenzyme binding sites to ... Chen, Z.; L.L.; Lee, W.R.; Chang, S.H. 1988: The coenzyme and substrate binding sites of alcohol dehydrogenase from drosophila ... Park, D.H.; Plapp, B.V. 1991: Isoenzymes of horse liver alcohol dehydrogenase active on ethanol and steroids. cDNA cloning, ... Pocker, Y.; De Roy, S.C. 1987: The active site of liver alcohol dehydrogenase mechanistic inferences from the binding and ...
In this study, diversity of alcohol dehydrogenases in Lactobacillus species was investigated with a focus on L. reuteri. Nine ... In this study, diversity of alcohol dehydrogenases in Lactobacillus species was investigated with a focus on L. reuteri. Nine ... Redox balance in Lactobacillus reuteri DSM20016 : Roles of iron-dependent alcohol dehydrogenases in glucose/glycerol metabolism ... the organism is likely to have alternative alcohol dehydrogenase(s) in the cytoplasm for transformation of the aldehyde. ...
a long-chain primary fatty alcohol + H2O + 2 NAD(+) <=> a long-chain fatty acid + 3 H(+) + 2 NADH. ...
phosphate dehydrogenase EC 1.1.1.140 *Sugar Alcohol Dehydrogenases. D-. ribose reductase EC 1.1.- *Sugar Alcohol Dehydrogenases ... Sugar Alcohol; Dehydrogenases, Sugar Alcohol; Alcohol Oxidoreductases, Sugar; Alcohol Dehydrogenases, Sugar ... Sugar Alcohol Dehydrogenases. Eur J Biochem 75(2):423,423;1977 glycerol dehydrogenase EC 1.1.1.6 *Sugar Alcohol Dehydrogenases. ... Sugar Alcohol Dehydrogenases. 1,5-. anhydro-. fructose reductase EC 1.1.1.- *Sugar Alcohol Dehydrogenases. J Biochem (Tokyo) ...
The coordination number of the catalytic zinc ion in alcohol dehydrogenase has been studied by integrated ab initio quantum ... The coordination of the catalytic zinc ion in alcohol dehydrogenase studied by combined quantum chemical and molecular ... proposals attributing an important role to five-coordinate zinc complexes in the catalytic mechanism of alcohol dehydrogenase. ...
Yasunami M, Kikuchi I, Sarapata D, Yoshida A: The human class I alcohol dehydrogenase gene cluster: three genes are tandemly ... Matsuo Y, Yokoyama S: Molecular structure of the human alcohol dehydrogenase 1 gene. FEBS Lett. 1989 Jan 16;243(1):57-60. ... Ikuta T, Szeto S, Yoshida A: Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary ... Gibbons BJ, Hurley TD: Structure of three class I human alcohol dehydrogenases complexed with isoenzyme specific formamide ...
"Alcohol Dehydrogenase" by people in this website by year, and whether "Alcohol Dehydrogenase" was a major or minor topic of ... "Alcohol Dehydrogenase" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and ... Below are the most recent publications written about "Alcohol Dehydrogenase" by people in Profiles. ...
The SCOP classification for the Iron-containing alcohol dehydrogenase family. Additional information, provided for both this ... INHERITED FROM: Glycerol dehydrogenase ,, sn-glycerol-1-phosphate dehydrogenase ,, Alcohol dehydrogenase. Enzyme Commission (EC ... Iron-containing alcohol dehydrogenase family. SCOP classification Root: SCOP hierarchy in SUPERFAMILY [. 0] (11) ... Glycerol dehydrogenase. 0.00000000001403. 3.23. --. DIRECT. Enzyme Commission (EC). Methanol dehydrogenase (nicotinoprotein). ...
Categorized as Alcohol Dehydrogenase However, the Th2 response triggered by cancer promotes the growth of cancer cells [34].  ... Categorized as Alcohol Dehydrogenase To verify the role for caspase-8 activation as an early event in panobinostat-induced ... Categorized as Alcohol Dehydrogenase The funders had no role in study design, data collection and analysis, decision to ... Categorized as Alcohol Dehydrogenase An dental dual inhibitor of PI3Kand PI3Kand are portrayed in every mammalian cells ...
... but in this lab the enzyme used is bovine alcohol dehydrogenase. This enzyme ... alcohol dehydrogenase can create upto nine different kinds of alcohol dehydrogenase each having different properties. For ... Catalytic activity of alcohol dehydrogenase: NADPH + an aldehyde NADP+ + an alcohol Methods: In order to conduct this ... According to its name Bovine alcohol dehydrogenase, which implicates that it is collectively formed from bovine (cow), alcohol ...
Detection and Quantification of Alcohol Dehydrogenase Activity.. Alternative Names: EC 1.1.1.1; Alcohol dehydrogenase; Aldehyde ... Alcohol dehydrogenase > Alcohol Dehydrogenase Microplate Assay Kit ...
Our ~2.7 Å structure of alcohol dehydrogenase (82 kDa) proves that bound ligands can be resolved with high fidelity to enable ... 2.7 Å resolution structure of 82 kDa alcohol dehydrogenase. We first decided to target the 82 kDa homodimeric enzyme alcohol ... Lyophilized horse liver alcohol dehydrogenase (Sigma Aldrich) (ADH) was solubilized in 20 mM HEPES (pH 7.5), 10 mM NaCl, 1 mM ... Our ~2.7 Å structure of alcohol dehydrogenase (82 kDa) proves that bound ligands can be resolved with high fidelity to enable ...
... form: FBgg0000926, label: ALCOHOL DEHYDROGENASES }, description: [ . ], comment: [] }, query: Get JSON for ... Open ALCOHOL DEHYDROGENASES in VFB. VFB Term Json. { term: { core: { iri: http://flybase.org/reports/FBgg0000926, ...
Although alcohol dehydrogenase is a naturally occurring enzyme in the liver, its protective effects could be bolstered by ... the curcumin supplements restricted the alcohol-induced inhibition of alcohol dehydrogenase activity to a statistically ... The activities of alcohol dehydrogenase resist these effects and limit damage.. Emerging research suggests that curcumin, the ... Although alcohol dehydrogenase is a naturally occurring enzyme in the liver, its protective effects could be bolstered by ...
Global Alcohol Dehydrogenase Market by Type:. 7.5 KU, 15 KU, 30 KU, 75 KU, 150 KU, Others. Global Alcohol Dehydrogenase market ... Global Alcohol Dehydrogenase Market 2020 Growth, Development and Forecast Report. *Home. *Global Alcohol Dehydrogenase Market ... Get a Alcohol Dehydrogenase Market Report Sample Copy @ https://www.industryandresearch.com/report/Global-Alcohol-Dehydrogenase ... Alcohol Dehydrogenase Market report is to recognize, explain and forecast the global market based on various aspects such as ...
The AdhEMeta protein most closely resembles the AdhE alcohol dehydrogenase of Clostridium acetobutylicum, where it catalyses ... Screening a Wide Host-Range Metagenomic Library from a Wastewater Treatment Plant Yields a Novel Alcohol/Aldehyde Dehydrogenase ... Screening a Wide Host-Range Metagenomic Library from a Wastewater Treatment Plant Yields a Novel Alcohol/Aldehyde Dehydrogenase ... Further, cell-free extracts of E. coli and R. leguminosarum containing cloned adhEMeta had butanol and ethanol dehydrogenase ...
Horse liver alcohol dehydrogenase with NAD and pentafluorobenzyl alcohol at 75 K ... Horse liver alcohol dehydrogenase with NAD and pentafluorobenzyl alcohol at 75 K Coordinates. PDB Format Method. X-RAY ... 2 x PFB: 2,3,4,5,6-PENTAFLUOROBENZYL ALCOHOL(Non-covalent). PFB.4: 14 residues within 4Å:*. Chain A: C.46, S.48, L.57, H.67, F. ... for complexes of horse liver alcohol dehydrogenases. Acta Crystallogr.,Sect.D (2022) Release Date. 2022-03-30. Peptides. ...
View Mouse Monoclonal anti-Sorbitol Dehydrogenase Antibody (OTI9E7) [Alexa Fluor® 405] (NBP2-74288AF405). Validated ... Although SORD is closely related to the class I long-chain alcohol dehydrogenases, it differs in substrate specificity, ... Additional Sorbitol Dehydrogenase Products. Array NBP2-74288AF405 * Sorbitol Dehydrogenase Antibodies. * Sorbitol Dehydrogenase ... Home » Sorbitol Dehydrogenase » Sorbitol Dehydrogenase Antibodies » Sorbitol Dehydrogenase Antibody (OTI9E7) [Alexa Fluor® 405] ...
... in which expression of the gene encoding cinnamyl alcohol dehydrogenase (CAD; EC 1.1.1.195) is severely reduced. The products ... Inheritance, gene expression, and lignin characterization in a mutant pine deficient in cinnamyl alcohol dehydrogenase. ... Inheritance, gene expression, and lignin characterization in a mutant pine deficient in cinnamyl alcohol dehydrogenase. ... in which expression of the gene encoding cinnamyl alcohol dehydrogenase (CAD; EC 1.1.1.195) is severely reduced. The products ...
Alcohol dehydrogenase (ADH) is an enzyme involved in pathways that respond to various environmental stresses such as osmotic, ... Mastura, Sani (2016) Heterologous expression of recombinant alcohol dehydrogenase gene from sago palm in bacterial and plant ... Heterologous expression of recombinant alcohol dehydrogenase gene from sago palm in bacterial and plant system ... Alcohol dehydrogenase, Heterologous expression, Insoluble and soluble protein, Agrobacterium tumefaciens, In planta ...
  • Deficient activity of the fatty aldehyde dehydrogenase component of fatty alcohol:NAD+ oxidoreductase in cultured fibroblasts. (jci.org)
  • To determine which enzymatic component of FAO was deficient in SLS, we assayed fatty aldehyde dehydrogenase (FALDH) and fatty alcohol dehydrogenase in cultured fibroblasts from seven unrelated SLS patients. (jci.org)
  • Moreover, evaluation of ADH6 deletion mutant showed strong decrease in ethanol level, supporting the role of this bifuctional alcohol/aldehyde dehydrogenase in ethanol production. (lu.se)
  • The main metabolic pathway for ethanol involves the enzymes alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). (nih.gov)
  • Aim: Aldehyde dehydrogenase 1 (ALDH1) has been advocated as a marker of alcohol intake. (wustl.edu)
  • A group with high activity of aldehyde dehydrogenase type 2 (EtOH = 143.3 ± 13.5 ppm, AcH = 1.7 ± 0.2 ppm) and a group with low activity (EtOH = 163.3 ± 28.0 ppm, AcH = 8.4 ± 0.5 ppm) displayed differences in the concentrations of EtOH and AcH contained in their breath samples, and the effectiveness of the developed method was confirmed and compared with previous results. (iitani.com)
  • Formaldehyde is subsequently metabolized via aldehyde dehydrogenase into formic acid, which ultimately is metabolized to folic acid, folinic acid, carbon dioxide, and water. (medscape.com)
  • In most of us, aldehyde dehydrogenase (ALDH) quickly metabolizes acetaldehyde to the inert acetate, which can be safely excreted. (medscape.com)
  • The researchers focused in on the aldehyde dehydrogenase enzyme and conducted a screening study. (medscape.com)
  • Mechanistic studies on equine liver alcohol dehydrogenase. (eurekamag.com)
  • cDNA and protein structure for the alpha subunit of human liver alcohol dehydrogenase. (t3db.ca)
  • For example in liver beta3 enzyme(Goodsell et al, 2001).These each enzyme is formed of two subunits and they can be mixed and match to create mixed dimerss which are more active.Alcohol dehdrogenates also modifies certain other alcohols with giving outcome of dangerous products such as methanol. (ukessays.com)
  • To better understand the causes of liver damage and support liver health, researchers have identified alcohol dehydrogenase as a critical site of inquiry. (tessmed.com)
  • Although alcohol dehydrogenase is a naturally occurring enzyme in the liver, its protective effects could be bolstered by curcumin supplementation, effectively supporting liver health. (tessmed.com)
  • the most common cause of liver damage in the United States is excessive alcohol intake, but a high-fat diet can also contribute to the condition, especially when it leads to obesity. (tessmed.com)
  • Currently, one particular target of research interest is alcohol dehydrogenase, an enzyme found primarily in the liver. (tessmed.com)
  • That makes alcohol dehydrogenase a key player in the detoxifying processes that protect the liver from damage. (tessmed.com)
  • Emerging research suggests that curcumin, the active compound in turmeric , supports the activity of alcohol dehydrogenase in a way that helps maintain a healthy liver. (tessmed.com)
  • This finding provided the first indication that it could be possible for curcumin to interact directly with the alcohol dehydrogenase enzymes in the human liver. (tessmed.com)
  • The strongest evidence for a direct relationship between curcumin and alcohol dehydrogenase, however, came in 2013, when a group of researchers from several universities in South Korea collaborated on an effort to investigate the protection that low doses of curcumin could provide against liver damage caused by chronic alcohol intake and a high-fat diet. (tessmed.com)
  • In addition to reducing the activity of the enzymes known to contribute to liver damage, the curcumin supplements restricted the alcohol-induced inhibition of alcohol dehydrogenase activity to a statistically significant degree. (tessmed.com)
  • Dependence of crystallographic atomic displacement factors on temperature (25-150 K) for complexes of horse liver alcohol dehydrogenases. (expasy.org)
  • The MDR superfamily with ~350-residue subunits contains the classical liver alcohol dehydrogenase (ADH), quinone reductase, leukotriene B4 dehydrogenase and many more forms. (researchgate.net)
  • Zinc binding to the peptide replica and analogs to residues 93-115 of horse liver alcohol dehydrogenase (ADH) was examined by competition of the peptides and the chromophoric chelator 4-(2- pyridylazo)resorcinol for zinc and X-ray absorption fine structure analysis of the zinc ligands. (researchgate.net)
  • [ 10 ] Methanol is primarily metabolized in the liver via alcohol dehydrogenase into formaldehyde. (medscape.com)
  • Long-term overuse of alcohol also increases the risk of certain cancers, including cancers of the mouth, throat, esophagus, liver, and breast. (medlineplus.gov)
  • Alcohol is metabolized by the enzyme alcohol dehydrogenase in the gut and then in the liver. (medscape.com)
  • Alcohol-Related Liver Disease Alcohol consumption is high in most Western countries. (msdmanuals.com)
  • the remainder is metabolized, mainly by the liver, where alcohol dehydrogenase converts ethanol to acetaldehyde. (msdmanuals.com)
  • BbsH, a member of the enoyl-CoA hydratase family, converts (E)-benzylidenesuccinyl-CoA to 2-(α-hydroxybenzyl)succinyl-CoA and was subsequently used in a coupled enzyme assay with BbsCD, which belongs to the short-chain dehydrogenases/reductase (SDR) family. (nih.gov)
  • Intriguingly, the unique curcumin-metabolizing enzyme they found (which they called NADPH-dependent curcumin/dihydrocurcumin reductase, or CurA), bore a significant sequence similarity to well-known enzymes in the alcohol dehydrogenase family. (tessmed.com)
  • Sorbitol dehydrogenase (SDH), a member of the medium-chain dehydrogenase/reductase protein family and the second enzyme of the polyol pathway of glucose metabolism, converts sorbitol to fructose strictly using NAD(+) as coenzyme. (novusbio.com)
  • Collectively, it forms alcohol dehydrogenase, which is ADH persuaded by ethanol and acetaldehyde as they relate to carbon catabolite repression. (ukessays.com)
  • The effects of beverage alcohol (ethanol) on the body are determined largely by the rate at which it and its main breakdown product, acetaldehyde, are metabolized after consumption. (nih.gov)
  • Because acetaldehyde has harmful effects on the body, people carrying these alleles are less likely to drink and have a lower risk of alcohol dependence. (nih.gov)
  • I say "most of us" because some populations, particularly those with East Asian ancestry, have a mutation in the ALDH gene which can lead to accumulation of toxic acetaldehyde with alcohol consumption - leading to facial flushing, nausea, and headache . (medscape.com)
  • The role of decreased gastric alcohol dehydrogenase activity and first-pass metabolism. (bvsalud.org)
  • women have lower gastric alcohol dehydrogenase activity than men. (msdmanuals.com)
  • Genetic evidence from comparisons of multiple organisms showed that a glutathione-dependent formaldehyde dehydrogenase, identical to a class III alcohol dehydrogenase (ADH-3/ADH5), is presumed to be the ancestral enzyme for the entire ADH family. (wikipedia.org)
  • In humans, sequencing of the ADH1B gene (responsible for production of an alcohol dehydrogenase polypeptide) shows several functional variants. (wikipedia.org)
  • In early 1960, the alcohol dehydrogenase (ADH) gene was discovered in fruit flies of the genus Drosophila melanogaster. (wikipedia.org)
  • Matsuo Y, Yokoyama S: Molecular structure of the human alcohol dehydrogenase 1 gene. (t3db.ca)
  • Yasunami M, Kikuchi I, Sarapata D, Yoshida A: The human class I alcohol dehydrogenase gene cluster: three genes are tandemly organized in an 80-kb-long segment of the genome. (t3db.ca)
  • Inheritance, gene expression, and lignin characterization in a mutant pine deficient in cinnamyl alcohol dehydrogenase. (ox.ac.uk)
  • The gene encoding a (2 R ,3 R )-2,3-butanediol dehydrogenase from Rhodococcus erythropolis WZ010 (ReBDH) was over-expressed in Escherichia coli and the resulting recombinant ReBDH was successfully purified by Ni-affinity chromatography. (mdpi.com)
  • Numerous studies have focused on the relationship be-tween alcohol dehydrogenase 1C gene ( ADH1C ) *1/*2 polymorphism (Ile350Val, rs698, also known as ADH1C *1/*2) and pancreatitis risk, but the results have been inconsistent. (geneticsmr.com)
  • Gene variations that result in skin flushing, nausea, headaches, and rapid heartbeat when drinking alcohol discourage its consumption and reduce the risk of alcohol use disorder. (medlineplus.gov)
  • An alcohol dehydrogenase 7 gene polymorphism associates with both acute and chronic pain in sickle cell disease. (cdc.gov)
  • This conversion involves three discrete enzymes: the microsomal cytochrome P450 isoenzyme CYP2E1, the cytosol-based enzyme alcohol dehydrogenase (ADH), and the peroxisome catalase system. (medscape.com)
  • Short-chain dehydrogenases/reductases (SDRs) constitute a large family of NAD(P)(H)-dependent oxidoreductases, sharing sequence motifs and displaying similar mechanisms. (researchgate.net)
  • Many alcohol dehydrogenases (ADHs) catalyze oxidation of a broad scope of alcohols. (rcsb.org)
  • Sjögren-Larsson syndrome (SLS) is an inherited disorder associated with impaired fatty alcohol oxidation due to deficient activity of fatty alcohol:NAD+ oxidoreductase (FAO). (jci.org)
  • FAO is a complex enzyme which consists of two separate proteins that sequentially catalyze the oxidation of fatty alcohol to fatty aldehyde and fatty acid. (jci.org)
  • Intact SLS fibroblasts oxidized octadecanol to fatty acid at less than 10% of the normal rate, but oxidized free octadecanal normally, suggesting that the FALDH affected in SLS is chiefly involved in the oxidation of fatty alcohol to fatty acid. (jci.org)
  • These results show that the primary enzymatic defect in SLS is the FALDH component of the FAO complex, which leads to deficient oxidation of fatty aldehyde derived from fatty alcohol. (jci.org)
  • Alcohol dehydrogenase contains a several isozymes which catalyze the oxidation of primary and secondary alcohols to convert into aldehydes and ketones (Arslanian et al, 1971). (ukessays.com)
  • Alcohol dehydrogenase is responsible for catalyzing the oxidation and reduction of various alcohols and aldehydes (organic molecules similar to alcohols, but with a slightly different molecular structure). (tessmed.com)
  • An engineered PQQ-dependent alcohol dehydrogenase for the oxidation of 5-(hydro. (rwth-aachen.de)
  • Alcohol accumulates in blood because absorption is more rapid than oxidation and elimination. (msdmanuals.com)
  • Genetic polymorphisms coding for alcohol dehydrogenase, the amount of alcohol consumed, and the rate at which ethanol is consumed all affect the speed of metabolism. (medscape.com)
  • Without competition for alcohol dehydrogenase, methanol undergoes zero-order metabolism, and is thus is excreted at a rate of 8.5 mg/dL/h to 20 mg/dL/h. (medscape.com)
  • Variations in genes that affect the metabolism (breakdown) of alcohol in the body have been studied as factors that can increase or decrease the risk of alcohol use disorder. (medlineplus.gov)
  • Characterization of cinnamyl alcohol dehydrogenase of Helicobacter pylori. (bvsalud.org)
  • 2008 ). As a complementary strategy to the traditional approach, it has been demonstrated that alcohol dehydrogenases (ADHs) can reduce such prochiral ketones with very high chemo-, regio-, and stereoselectivity, thereby enabling a sustainable synthetic route to chiral alcohols, which includes biodegradability of the biocatalyst (Garcia-Urdiales et al. (springeropen.com)
  • There are currently no images for Sorbitol Dehydrogenase Antibody (NBP2-74288AF405). (novusbio.com)
  • Full length recombinant protein of human Sorbitol Dehydrogenase (NP_003095) produced in HEK293T cells. (novusbio.com)
  • Methods: ALDH activity was measured in erythrocytes from 677 men and women who had participated in a twin study of alcohol use and dependence. (wustl.edu)
  • Results: There were no significant effects of sex, alcohol consumption or alcohol dependence on ALDH activity. (wustl.edu)
  • These by products are converted into formaldehyde by help of alcohol dehydrogenase (Goodsell et al, 2001). (ukessays.com)
  • abstract = "Monoamine oxidase (MAO) and alcohol dehydrogenase (AD) activities were studied histochemically in the Syrian hamster Harderian gland using tryptamine as substrate and Nitroblue Tetrazolium as the final electron acceptor. (uthscsa.edu)
  • Ikuta T, Szeto S, Yoshida A: Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence. (t3db.ca)
  • This provides some protection against excessive alcohol consumption and alcohol dependence (alcoholism). (wikipedia.org)
  • This led to speculation that increased alcohol availability led to alcoholism and abuse, resulting in lower reproductive fitness. (wikipedia.org)
  • Alcohol and Alcoholism , 40 (5), 343-348. (wustl.edu)
  • It includes alcoholism, also called alcohol addiction, which is a long-lasting (chronic) condition characterized by a powerful, compulsive urge to drink alcohol and the inability to stop drinking after starting. (medlineplus.gov)
  • In addition to alcoholism, alcohol use disorder includes alcohol abuse, which involves problem drinking without addiction. (medlineplus.gov)
  • When an NAD-dependent ADH oxidizes methanol, albeit at a poor rate, it may be treated as methanol dehydrogenase (MDH). (rcsb.org)
  • Although any alcohol can be toxic if ingested in large enough quantities, the term toxic alcohol has traditionally referred to isopropanol, methanol, and ethylene glycol. (medscape.com)
  • Wine headaches are on my mind this week, not only because of the incoming tide of Beaujolais nouveau, but because of a new study which claims to have finally explained the link between wine consumption and headaches - and apparently it's not just the alcohol. (medscape.com)
  • For most drinkers, the frequency and amount of alcohol consumption does not impair physical or mental health or the ability to safely carry out daily activities. (msdmanuals.com)
  • In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. (wikipedia.org)
  • Though this feature is not adaptive from an energy point of view, by making alcohol in such high concentrations so that they would be toxic to other organisms, yeast cells could effectively eliminate their competition. (wikipedia.org)
  • The first-ever isolated alcohol dehydrogenase (ADH) was purified in 1937 from Saccharomyces cerevisiae (brewer's yeast). (wikipedia.org)
  • So overall, alcohol dehydrogenase converts potentially dangerous molecule into food ustilized by the cells preent within the body.In human bidy, alcohol dehydrogenase can create upto nine different kinds of alcohol dehydrogenase each having different properties. (ukessays.com)
  • Habitual excessive use of alcohol changes the chemistry of the brain and leads to tolerance, which means that over time the amount of alcohol ingested needs to be increased to achieve the same effect. (medlineplus.gov)
  • All SLS cells were selectively deficient in the FALDH component of FAO, and had normal activity of fatty alcohol dehydrogenase. (jci.org)
  • Detection and Quantification of Alcohol Dehydrogenase Activity. (biotrend.com)
  • Although SORD is closely related to the class I long-chain alcohol dehydrogenases, it differs in substrate specificity, catalyzing polyols such as sorbitol and xylitol but having no activity towards primary alcohols. (novusbio.com)
  • This study tested whether variation in erythrocyte ALDH1 activity was associated with alcohol use, alcohol dependence or reactions to alcohol in unselected subjects of European descent, and whether variation in ALDH1 activity was subject to genetic influences. (wustl.edu)
  • Subjects who reported reactions to alcohol did not have low activity. (wustl.edu)
  • The coordination number of the catalytic zinc ion in alcohol dehydrogenase has been studied by integrated ab initio quantum chemical and molecular mechanical geometry optimisations involving the whole enzyme. (lu.se)
  • The purified ReBDH in the native form was found to exist as a monomer with a calculated subunit size of 37180, belonging to the family of the zinc-containing alcohol dehydrogenases. (mdpi.com)
  • In this study, diversity of alcohol dehydrogenases in Lactobacillus species was investigated with a focus on L. reuteri. (lu.se)
  • Thus, the results give no support to proposals attributing an important role to five-coordinate zinc complexes in the catalytic mechanism of alcohol dehydrogenase. (lu.se)
  • A thermostable alcohol dehydrogenase from Thermoanaerobacter brockii (TbSADH) has been repurposed to perform asymmetric reduction of a series of prochiral ketones with the formation of enantio-pure secondary alcohols, which are crucial chiral synthons needed in the preparation of various pharmaceuticals. (springeropen.com)
  • Gibbons BJ, Hurley TD: Structure of three class I human alcohol dehydrogenases complexed with isoenzyme specific formamide inhibitors. (t3db.ca)
  • Since L. reuteri excretes high amounts of 3-HPA outside the microcompartment, the organism is likely to have alternative alcohol dehydrogenase(s) in the cytoplasm for transformation of the aldehyde. (lu.se)
  • Various haplotypes arising from this mutation are more concentrated in regions near Eastern China, a region also known for its low alcohol tolerance and dependence. (wikipedia.org)
  • Those with the variant allele have little tolerance for alcohol, thus lowering chance of dependence and abuse. (wikipedia.org)
  • Chronic heavy alcohol use can also cause long-term problems affecting many organs and systems of the body. (medlineplus.gov)
  • Chronic alcohol abuse interferes with the ability to socialize and work. (msdmanuals.com)
  • In the world of chemistry, there are millions of enzymes, but in this lab the enzyme used is bovine alcohol dehydrogenase. (ukessays.com)
  • Alcohol Dehydrogenase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (wakehealth.edu)