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.
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.
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.-.
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.
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.
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).
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.
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.
(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)
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.
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.
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)
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.
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)

TY - JOUR. T1 - Class IV mammalian alcohol dehydrogenase. Structural data of the rat stomach enzyme reveal a new class well separated from those already characterized. AU - Parés, Xavier. AU - Moreno, Alberto. AU - Cederlund, Ella. AU - Höög, Jan Olov. AU - Jörnvall, Jans. PY - 1990/12/17. Y1 - 1990/12/17. N2 - The stomach form of alcohol dehydrogenase has been structurally evaluated by peptide analysis covering six separate regions of the rat enzyme. Overall, this new structure diners widely (32-40% residue differences) from the structures of three classes of alcohol dehydrogenase characterized before from the same species. Consequently, this novel enzyme constitutes a true fourth class of mammalian alcohol dehydrogenase. In particular, differences are extensive also towards class II, although enzymatic and physicochemical properties initially suggested overall similarities with class II. The new structure establishes the presence of one further alcohol dehydrogenase mammalian gene, extends ...
Mammalian alcohol dehydrogenase (ADH) constitutes a complex system with different forms and extensive multiplicity (ADH1-ADH6) that catalyze the oxidation and reduction of a wide variety of alcohols...
Définitions de 1 3 propanediol dehydrogenase, synonymes, antonymes, dérivés de 1 3 propanediol dehydrogenase, dictionnaire analogique de 1 3 propanediol dehydrogenase (anglais)
Alcohol dehydrogenases (ADH) (EC 1.1.1.1) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in generation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. 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. Early on in evolution, an effective method for eliminating both endogenous and exogenous formaldehyde was important and this ...
The best strategy for providing food and maintaining the environment on long-duration space missions is a bioregenerative life support system based on the growth of higher plants. Before such a system can be implemented, a better understanding of plant growth in space will have to be achieved. Little is known about the role of gravity-dependent physical processes in normal physiological function. A series of ground-based and spaceflight experiments was conducted to examine root oxygen availability in microgravity nutrient delivery systems. In spaceflight experiments Arabidopsis thaliana (L.) Heynh. plants were analyzed for changes in root medium redox potential and root alcohol dehydrogenase (ADH) activity, localization, and expression. These experiments showed ADH activity and expression increased by 89% and 136% respectively, without any change in localization. Ground experiments demonstrated the increase in ADH activity in spaceflight roots was achieved by a 28% decrease in oxygen availability.
The Saccharomyces cerevisiae nuclear gene, ADH3, that encodes the mitochondrial alcohol dehydrogenase isozyme ADH III was cloned by virtue of its nucleotide homology to ADH1 and ADH2. Both chromosomal and plasmid-encoded ADH III isozymes were repressed by glucose and migrated heterogeneously on nondenaturing gels. Nucleotide sequence analysis indicated 73 and 74% identity for ADH3 with ADH1 and ADH2, respectively. The amino acid identity between the predicted ADH III polypeptide and ADH I and ADH II was 79 and 80%, respectively. The open reading frame encoding ADH III has a highly basic 27-amino-acid amino-terminal extension relative to ADH I and ADH II. The nucleotide sequence of the presumed leader peptide has a high degree of identity with the untranslated leader regions of ADH1 and ADH2 mRNAs. A strain containing a null allele of ADH3 did not have a detectably altered phenotype. The cloned gene integrated at the ADH3 locus, indicating that this is the structural gene for ADH III. ...
Background: All known attempts to isolate and characterize mammalian class V alcohol dehydrogenase (class V ADH), a member of the large ADH protein family, at the protein level have failed. This indicates that the class V ADH protein is not stable in a non-cellular environment, which is in contrast to all other human ADH enzymes. In this report we present evidence, supported with results from computational analyses performed in combination with earlier in vitro studies, why this ADH behaves in an atypical way. Results: Using a combination of structural calculations and sequence analyses, we were able to identify local structural differences between human class V ADH and other human ADHs, including an elongated beta-strands and a labile a-helix at the subunit interface region of each chain that probably disturb it. Several amino acid residues are strictly conserved in class I-IV, but altered in class V ADH. This includes a for class V ADH unique and conserved Lys51, a position directly involved ...
class I, II, IV alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. This group includes alcohol dehydrogenases corresponding to mammalian classes I, II, IV. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, ...
After consumption, alcohol is mostly absorbed in the upper GI tract and then enters the liver via the portal vein. However, contrary to popular belief, some of it still does reach the distal small intestine, and concentrations close to the colon within an hour of drinking 2.5 standard drinks (0.8g/kg) were shown to reach 200mg/ml.[1] The majority of alcohol metabolism occurs in cells called hepatocytes, contained in the liver. At lower levels of consumption (average of 2 drinks), the body breaks down the alcohol through a process called oxidative conversion, where the enzyme alcohol dehydrogenase (ADH) turns it into the toxic compound acetaldehyde. This is then converted into acetate by another enzyme, acetaldehyde dehydrogenase (ALDH). In each step, NAD+ is reduced to NADH, resulting in the production of some reactive oxygen species. This process typically results in few negative side effects.[2] When larger amounts of alcohol are consumed, another metabolic pathway is used, known as the ...
Alcohol dehydrogenase 4 is an enzyme that in humans is encoded by the ADH4 gene. This gene encodes class II alcohol dehydrogenase 4 pi subunit, which is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. Class II alcohol dehydrogenase is a homodimer composed of 2 pi subunits. It exhibits a high activity for oxidation of long-chain aliphatic alcohols and aromatic alcohols and is less sensitive to pyrazole. This gene is localized to chromosome 4 in the cluster of alcohol dehydrogenase genes. GRCh38: Ensembl release 89: ENSG00000198099 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000037797 - Ensembl, May 2017 Human PubMed Reference:. Mouse PubMed Reference:. Entrez Gene: ADH4 alcohol dehydrogenase 4 (class II), pi polypeptide. Human ADH4 genome location and ADH4 gene details page in the UCSC Genome Browser. ...
Humans metabolize ethanol primarily through NAD+-dependent alcohol dehydrogenase (ADH) class I enzymes (i.e. ADH1A, ADH1B, and ADH1C) to acetaldehyde and then metabolize acetaldehyde primarily by NAD2-dependent aldehyde dehydrogenase 2 (ALDH2) to acetic acid.[27][28] Eastern Asians reportedly have a deficiency in acetaldehyde metabolism in a surprisingly high percentage (approaching 50%) of their populations. The issue has been most thoroughly investigated in native Japanese where persons with a single-nucleotide polymorphism (SNP) variant allele of the ALDH2 gene were found; the variant allele, encodes lysine (lys) instead of glutamic acid (glu) at amino acid 487; this renders the enzyme essentially inactive in metabolizing acetaldehyde to acetic acid.[29][30] The variant allele is variously termed glu487lys, ALDH2*2, and ALDH2*504lys. In the overall Japanese population, about 57% of individuals are homozygous for the normal allele (sometimes termed ALDH2*1), 40% are heterozygous for glu487lys, ...
Humans metabolize ethanol primarily through NAD+-dependent alcohol dehydrogenase (ADH) class I enzymes (i.e. ADH1A, ADH1B, and ADH1C) to acetaldehyde and then metabolize acetaldehyde primarily by NAD2-dependent aldehyde dehydrogenase 2 (ALDH2) to acetic acid.[26][27] Eastern Asians reportedly have a deficiency in acetaldehyde metabolism in a surprisingly high percentage (approaching 50%) of their populations. The issue has been most thoroughly investigated in native Japanese where persons with a single-nucleotide polymorphism (SNP) variant allele of the ALDH2 gene were found; the variant allele, encodes lysine (lys) instead of glutamic acid (glu) at amino acid 487; this renders the enzyme essentially inactive in metabolizing acetaldehyde to acetic acid.[28][29] The variant allele is variously termed glu487lys, ALDH2*2, and ALDH2*504lys. In the overall Japanese population, about 57% of individuals are homozygous for the normal allele (sometimes termed ALDH2*1), 40% are heterozygous for glu487lys, ...
The retention of the enzyme activity of alcohol dehydrogenase (ADH) has been studied in various drying processes such as spray drying. The aim of this study is to encapsulate ADH in mannitol, either with or without additive in order to limit the thermal denaturation of the enzyme during the drying process. The retention of ADH activity was investigated at different drying temperatures. When mannitol was used, the encapsulated ADH was found inactive in all the dried powders. This is presumably due to the quick crystallization of mannitol during spray drying that resulted in the impairment of enzyme protection ability in comparison to its amorphous form. Maltodextin (dextrose equivalent = 11) was used to reduce the crystallization of mannitol. The addition of maltodextrin increased ADH activity and drastically changed the powder X-ray diffractogram of the spray-dried powders.
Enzymatic synthesis of enantiopure aromatic secondary alcohols (including substituted, heteroaromatic and bicyclic structures) were carried out using the halophilic alcohol dehydrogenase ADH2 from Haloferax volcanii (HvADH2). This enzyme showed an unprecedented substrate scope and absolute enatioselectivity. The cofactor NADPH was used catalytically and regenerated in-situ by the biocatalyst, in the presence of 5% ethanol. The efficiency of HvADH2 for conversion of aromatic ketones was markedly influenced by the steric and electronic factors as well as the solubility of ketones in the reaction medium. Furthermore, carbonyl stretching bands frequencies ν ( ) have been measured for different ketones to understand the effect of electron withdrawing or donating properties of the ketones substituents on the reaction rate catalyzed by HvADH2. Good correlation was observed between ν ( ) of methyl aryl-ketones and the reaction rate catalyzed by HvADH2. The enzyme catalyzed the reductions of ketone ...
TY - JOUR. T1 - Molecular systematics of the genus Neotoma based on DNA sequences from intron 2 of the alcohol dehydrogenase gene. AU - Bradley, Robert. AU - Longhofer, Lisa. PY - 2006. Y1 - 2006. M3 - Article. JO - Journal of Mammalogy. JF - Journal of Mammalogy. ER - ...
TY - JOUR. T1 - Regulation of the expression of the rat alcohol dehydrogenase gene by glucocorticoids.. AU - Qulali, M.. AU - Wolfla, C. E.. AU - Ross, R. A.. AU - Crabb, D. W.. PY - 1989. Y1 - 1989. UR - http://www.scopus.com/inward/record.url?scp=0024491855&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0024491855&partnerID=8YFLogxK. M3 - Article. C2 - 2471210. AN - SCOPUS:0024491855. VL - 290. SP - 143. EP - 153. JO - Progress in Clinical and Biological Research. JF - Progress in Clinical and Biological Research. SN - 0361-7742. ER - ...
Seversal short-chain alcohols, especially ethanol, is abundent in the natural habitats of Drosophilu melanogaster and alcohol dehydrogenase (ADH) plays a key role in the detoxification ethanol and other alcohols. In general, primary alcohols are converted to aldehydes, and secondary alcohols to ketones by ADH. The purpose of this study is to define the function and regulation mechanism of Adh gene by examing how dietary threonine effects on the expression of the Adh gene during the development of Drosophilu melanogaster. In this study, two other wild type strain, one homozygous for Adh^(F) and one for Adh^(S), from Chunan Korea were used. ADH activity was measured by spectrophotometric method and ADH CRMs was calculated by using radial immunodiffusion. To exam the Adh gene expression, northern hybridization analysis was carried. The rusults obtained were as follows: The activities of Adh^(F) strain were about two fold higher than Adh^(S) strain and ADH CRMs were about 1.5 fold higher. ADH ...
Oksidoreduktase alkohol:NAD+ (bahasa Inggris: aldehyde reductase; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase, NAD+ oxidoreductase, ADH; EC 1.1.1.1) adalah keluarga enzim dari golongan dehidrogenase yang berfungsi sebagai katalisator oksidasi alkohol dengan aldehid atau keton, dengan reduksi NAD+ menjadi NADH. ADH merupakan protein yang mengandung Zn yang bereaksi pada alkohol primer dan sekunder atau asetal-hemi, dan alkohol sekunder siklik.[1] Reaksi yang terjadi: ...
Tobacco plants were transformed with a Nhap type Na,sup,+,/sup,/H,sup,+,/sup, antiporter gene, ,i,SynnhaP1,/i, (slr1595), from a cyanobacterium ,i,Synechocystis,/i, sp. PCC 6803. Two kinds of promoters, ,i,Arabidopsis,/i, alcohol dehydrogenase gene promoter (Adh promoter) and CaMV 35S promoter (35S promoter), were used. The transgenic plants driven by Adh promoter accumulated SynNhaP1 proteins only in root whereas the transgenic plants driven by 35S promoter accumulated SynNhaP1 proteins in all tissues. Confocal imaging of SynNhaP1-GFP fusion protein suggests the intracellular localization of SynNhaP1 in plasma membrane. Transgenic plants exhibited higher germination yields, increased biomass during developmental stage, increased seed production, and decreased intracellular Na,sup,+,/sup, content under salt-stress conditions. The transgenic plants driven by Adh promoter exhibited similar or slightly higher salt tolerance than that by 35S promoter. These results indicate the importance of ...
Multifactorial approaches can quickly and efficiently model complex, interacting natural or engineered biological systems in a way that traditional one-factor-at-a-time experimentation can fail to do. We applied a Design of Experiments (DOE) approach to model ethanol biosynthesis in yeast, which is well-understood and genetically tractable, yet complex. Six alcohol dehydrogenase (ADH) isozymes catalyze ethanol synthesis, differing in their transcriptional and post-translational regulation, subcellular localization, and enzyme kinetics. We generated a combinatorial library of all ADH gene deletions and measured the impact of gene deletion(s) and environmental context on ethanol production of a subset of this library. The data were used to build a statistical model that described known behaviors of ADH isozymes and identified novel interactions. Importantly, the model described features of ADH metabolic behavior without explicit a priori knowledge. The method is therefore highly suited to ...
The structural framework of cod liver alcohol dehydrogenase is similar to that of horse and human alcohol dehydrogenases. In contrast, the substrate pocket differs significantly, and main differences are located in three loops. Nevertheless, the substrate pocket is hydrophobic like that of the mammalian class I enzymes and has a similar topography in spite of many main-chain and side-chain differences. The structural framework of alcohol dehydrogenase is also present in a number of related enzymes like glucose dehydrogenase and quinone oxidoreductase. These enzymes have completely different substrate specificity, but also for these enzymes, the corresponding loops of the substrate pocket have significantly different structures. The domains of the two subunits in the crystals of the cod enzyme further differ by a rotation of the catalytic domains by about 6 degrees. In one subunit, they close around the coenzyme similarly as in coenzyme complexes of the horse enzyme, but form a more open cleft in ...
S-nitrosoglutathione reductase (GSNOR), or ADH5, is an enzyme in the alcohol dehydrogenase (ADH) family. It is unique when compared to other ADH enzymes in that primary short-chain alcohols are not its principle substrate ...
Expression-ready Human ADH5 cDNA ORF clone (HG17057-NY) with enhanced promotor in expression vector (pCMV3-N-HA) is confirmed by full-length sequence and validated in expression capability for gene expression studies or other applications. Quote for bulk production.
References for Abcams Recombinant Human ADH5 protein (ab124573). Please let us know if you have used this product in your publication
Alcohol, as a toxin, can result in cellular damage after prolonged effects. The first step toward metabolizing alcohol is to convert it to acetaldehyde. It has been found that 50% of the Pacific Rim Asian population (Chinese, Japanese, Koreans) possess an atypical alcohol dehydrogenase (ADH) known as ADH2*2 that leads to unusually rapid conversion of ethanol to acetaldehyde. This atypical ADH is less expressed in Caucasians, Africans Americans, Native Americans, and Asian Indian (Agarwal and Goedde, 1992). Since acetaldehyde is more toxic than alcohol, its increased accumulation causes flushing in the human body. Moreover, the normal aldehyde dehydrogenase (ALDH2), synthesized in the liver, oxidizes acetaldehyde into a carboxylic acid, acetic acid.[3] Mutant ALDH2 enzyme (known as ALDH2*2) in 45 to 53 percent of Japanese, Chinese, Korean, Taiwanese, and Vietnamese population, however, is only 8% as effective as the normal, wild-type enzyme (ALDH*1). This mutant allele of ALDH2 is dominant, as it ...
In the liver, ethanol is predominantly metabolised by alcohol dehydrogenase (ADH) and CYP 2E1, resulting in acetaldehyde (AA) formation. AA, the extremely toxic first intermediate of ethanol metabolism, binds rapidly to cellular proteins and also possibly to DNA. These AA adducts represent neoantigens leading to the formation of specific antibodies.26 AA has mutagenic and carcinogenic properties leading to metaplasia, inhibition of DNA repair,27 sister chromatid exchanges,28 stimulation of apoptosis, and enhanced cell injury associated with hyperregeneration.29 According to the International Agency for Research on Cancer, there is sufficient evidence to identify AA as a carcinogen in animals.. Ethanol is metabolised by the successive action of ADH and aldehyde dehydrogenase (ALDH). For both ADH and ALDH, genetic polymorphisms have been described that influence the rate of conversion of ethanol to AA and of the latter to acetate.30 It has been consistently reported that ALDH2 is the most ...
We have tested for effects of alcohol dehydrogenase (ADH) genotypes on self-reported alcohol consumption and symptoms of alcohol dependence, recorded on three occasions up to 15 years apart, in 377 male and female subjects of European descent. ADH2 genotype had significant effects on both consumptio …
Alzheimers disease ; Beta-amyloid ; Aß-binding alcohol dehydrogenase (ABAD) ; Receptor for advanced glycation end products (RAGE) ; QP552.A45R4 ; Amyloid beta-protein ; Alcohol dehydrogenase ; Cell receptors ; Alzheimers disease
The transcriptional activator ADR1 from Saccharomyces cerevisiae is a postulated DNA-binding protein that controls the expression of the glucose-repressible alcohol dehydrogenase (ADH2). Carboxy-terminal deletions of the ADR1 protein (1,323 amino acids in length) were used to localize its functional regions. The transcriptional activation region was localized to the N-terminal 220 amino acids of ADR1 containing two DNA-binding zinc finger motifs. In addition to the N terminus, a large part of the ADR1 sequence was shown to be essential for complete activation of ADH2. Deletion of the putative phosphorylation region, defined by ADR1c mutations that overcome glucose repression, did not render ADH2 expression insensitive to glucose repression. Instead, this region (amino acids 220 through 253) was found to be required by ADR1 to bypass glucose repression. These results suggest that ADR1c mutations enhance ADR1 function, rather than block an interaction of the putative phosphorylation region with a ...
Paleogenetics is an emerging field that resurrects ancestral proteins from now-extinct organisms to test, in the laboratory, models of protein function based on natural history and Darwinian evolution. Here, we resurrect digestive alcohol dehydrogenases (ADH4) from our primate ancestors to explore the history of primate-ethanol interactions. The evolving catalytic properties of these resurrected enzymes show that our ape ancestors gained a digestive dehydrogenase enzyme capable of metabolizing ethanol near the time that they began using the forest floor, about 10 million y ago. The ADH4 enzyme in our more ancient and arboreal ancestors did not efficiently oxidize ethanol. This change suggests that exposure to dietary sources of ethanol increased in hominids during the early stages of our adaptation to a terrestrial lifestyle. Because fruit collected from the forest floor is expected to contain higher concentrations of fermenting yeast and ethanol than similar fruits hanging on trees, this ...
TY - JOUR. T1 - Hominids adapted to metabolize ethanol long before human-directed fermentation. AU - Carrigan, Matthew A.. AU - Uryasev, Oleg. AU - Frye, Carole B.. AU - Eckman, Blair L.. AU - Myers, Candace R.. AU - Hurley, Thomas D.. AU - Benner, Steven A.. PY - 2015/1/13. Y1 - 2015/1/13. N2 - Paleogenetics is an emerging field that resurrects ancestral proteins from now-extinct organisms to test, in the laboratory, models of protein function based on natural history and Darwinian evolution. Here, we resurrect digestive alcohol dehydrogenases (ADH4) from our primate ancestors to explore the history of primate-ethanol interactions. The evolving catalytic properties of these resurrected enzymes show that our ape ancestors gained a digestive dehydrogenase enzyme capable of metabolizing ethanol near the time that they began using the forest floor, about 10 million y ago. The ADH4 enzyme in our more ancient and arboreal ancestors did not efficiently oxidize ethanol. This change suggests that ...
Transgenic arabidopsis plants containing the alcohol dehydrogenase (Adh) gene promoter fused to the green fluorescent protein (GFP) reporter gene were developed as biological sensors for monitoring physiological responses to unique environments. Plan
Ruth, like many Asian Americans, has at times been reluctant to drink wine because of her tendency to turn a deep shade of red after even just half a glass of red or white.. The cause of this wine flush has to do with how many Asians metabolize alchohol. Alchohol is absorbed through the stomach and small intestine. About 10 percent is eliminated by the kidneys, lungs, and sweat glands, but the rest is dealt with in the liver by two enzymes: alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). I dont know enough about the bodys chemistry to know how these two enzymes actually manage to break down the alchohol, but its enough to know that they do.. Its this second enzyme (ALDH) that is missing (or low) in up to 50 percent of Asian people, and is not present at all in most Native Americans and Inuits. People with less ALDH will often flush and sweat after drinking alcohol, and if their quantities of the enzyme are quite low, they may also become ill after drinking even small amounts ...
1. The excretion of H+ ions, with practically equivalent uptake of K+ ions (from 0·1m-potassium chloride), occurs during the aerobic oxidation of ethanol. 2. Acetaldehyde and acetic acid formed at the same time are quantitatively equal to the amount of ethanol oxidized. 3. A slow uptake of K+ ions occurs during the oxidation of acetaldehyde and a more rapid uptake during the oxidation of d-glyceraldehyde 3-phosphate. 4. The anaerobic reduction of methylene blue is studied, and the inhibitory effect of K+ and other inorganic cations on the system demonstrated. 5. The cation requirement for equal inhibitory effect is parallel with the reciprocals of the transport affinities for the physiological K-carrier (as taken from Conway & Duggan, 1958). 6. The cation inhibition of methylene blue reduction is reversed by treatment of the yeast with Teepol or by freezing-and-thawing. 7. Azide is shown to inhibit the reduction of methylene blue with intact cells. The inhibition is partially reversed by ...
SWISS-MODEL Template Library (SMTL) entry for 3cos. Crystal structure of human class II alcohol dehydrogenase (ADH4) in complex with NAD and Zn
SORD [ENSP00000267814]. L-iditol 2-dehydrogenase; Converts sorbitol to fructose. Part of the polyol pathway that plays an important role in sperm physiology. May play a role in the sperm motility by providing an energetic source for sperm; Belongs to the zinc-containing alcohol dehydrogenase family.. Synonyms: SORD, B7Z3A6, H0YKB3, H0YLA4, Q00796 .... Linkouts: STRING Pharos UniProt OMIM ...
Accepted name: alcohol dehydrogenase (nicotinoprotein). Reaction: ethanol + acceptor - acetaldehyde + reduced acceptor. Other name(s): nicotinoprotein alcohol dehydrogenase; np-ADH; NDMA-dependent alcohol dehydrogenase; ethanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase. Systematic name: ethanol:acceptor oxidoreductase. Comments: Contains Zn2+. Nicotinoprotein alcohol dehydrogenases are unique medium-chain dehydrogenases/reductases (MDR) alcohol dehydrogenases that have a tightly bound NAD+/NADH cofactor that does not dissociate during the catalytic process. Instead, the cofactor is regenerated by a second substrate or electron carrier. While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA), which is reduced to 4-(hydroxylamino)-N,N-dimethylaniline, can serve this function in vitro. The enzyme from the Gram-positive bacterium Amycolatopsis methanolica can accept many primary alcohols as substrates, including benzylalcohol [1].. Links to other databases: BRENDA, ...
Alcohol use that begins during adolescence affects the development of alcohol use disorders during adulthood. A new study looks at the effects of interplay between peer drinking and the functional variant rs1229984 in the alcohol dehydrogenase 1B gene (ADH1B) among adolescents. Peer drinking reduces the protective effects of this ADH1B variant.
Kit contents: 1. MICROTITER PLATE * 1 2. ENZYME CONJUGATE*1 vial 3. STANDARD A*1 vial 4. STANDARD B*1 vial 5. STANDARD C*1 vial 6. STANDARD D*1 vial 7. STANDARD E*1 vial 8. STANDARD F*1 vial 9. SUBSTRATE A*1 vial 10. SUBSTRATE B*1 vial 11. STOP ...
Three anti-horse liver alcohol dehydrogenase (HLADH) monoclonal antibodies are described. Two are specific for ADH and cross-react with class I and II enzymes from mouse, horse and Chinese hamster....
1MGO: Mobility of Fluorobenzyl Alcohols Bound to Liver Alcohol Dehydrogenases as Determined by NMR and X-ray Crystallographic Studies
1A72: Active site modifications in a double mutant of liver alcohol dehydrogenase: structural studies of two enzyme-ligand complexes.
Vanillin is a potent fermentation inhibitor derived from the lignocellulosic biomass in biofuel production, and high concentrations of vanillin result in the pronounced repression of bulk translation in Saccharomyces cerevisiae. Studies on genes that are efficiently translated even in the presence of high concentrations of vanillin will be useful for improving yeast vanillin tolerance and fermentation efficiency. The BDH1 and BDH2 genes encode putative medium-chain alcohol dehydrogenase/reductases and their amino acid sequences are very similar to each other. Although BDH2 was previously suggested to be involved in vanillin tolerance, it has yet to be clarified whether Bdh1/Bdh2 actually contribute to vanillin tolerance and reductions in vanillin. Therefore, we herein investigated the effects of Bdh1 and Bdh2 on vanillin tolerance. bdh2Δ cells exhibited hypersensitivity to vanillin and slower reductions in vanillin than wild-type cells and bdh1Δ cells. Additionally, the overexpression of the BDH2 gene
If your face goes red when drinking alcohol, youre not alone. More than one in three people with East Asian heritage (Chinese, Japanese, and Korean) experience facial flushing when drinking beer, wine, or spirits.. In Asian populations, it is due to an inherited deficiency in one of the enzymes involved in the breakdown of alcohol: aldehyde dehydrogenase. This type of reaction is very rare, but not unknown, in other ethnic groups.. But there is more to this deficiency than just an embarrassing reddening of the face. There are positive and negative health implications. And it provided a lightbulb moment, helping us understand how a common treatment for alcoholism works.. How you digest alcohol. Alcohol is broken down in your liver in two steps. In the first step, the enzyme alcohol dehydrogenase converts alcohol into a rather nasty chemical called acetaldehyde. A build up of this toxic chemical is one of the reasons you feel sick when hungover.. Then a second enzyme, aldehyde dehydrogenase, ...
My research centers on molecular population genetics and evolution. I am interested in understanding the evolutionary basis for high levels of polymorphisms within species, and in determining whether natural selection contributes to the maintenance of within- species variation. I am also interested in knowing whether molecular evolution between species results from the same evolutionary forces that produce intra-species variation. Using the alcohol dehydrogenase locus (Adh) as a model system, our studies reveal how selection has contributed to the evolution of the locus over three time scales: affecting populations, affecting species, and affecting long-term molecular evolution. Finally, because our ability to acquire molecular data is limited by technology, I place a special emphasis on developing better methods for measuring genetic variation. Current projects in the lab include the role of natural selection in the evolution of codon nias, the relationship between recombination rates and ...
The present study discusses the metabolism of ethanol in the human body from the ingestion of ethanol to the excretion of its break down products water and carbon dioxide. Ethanol is a small molecule, soluble in water as well as in organic solutions. It is quickly distributed to every section in the body, where it exerts a direct toxic effect on the cells. Ethanol cannot directly leave the body efficiently so it needs other metabolic pathways. The molecule is metabolized by oxidation, predominately in the liver. The enzyme alcohol dehydrogenase catalyses the degradation of ethanol to acetaldehyde. Acetaldehyde is even more toxic than ethanol and it is degraded by the enzyme aldehyde dehydrogenase. In chronic alcoholics other chemical processes such as the cytochrome P450 system may have a bigger impact on alcohol metabolism.. The carbohydrate metabolism is extensively affected by ethanol. Most important is its restrictive effect on the gluconeogenesis leading to sustained hypoglycaemia in ...
The pattern that we developed to detect this class of enzymes is based on a conserved region that includes a histidine residue which is the second ligand of the catalytic zinc atom. This family also includes NADP-dependent quinone oxidoreductase (EC 1.6.5.5), an enzyme found in bacteria (gene qor), in yeast and in mammals where, in some species such as rodents, it has been recruited as an eye lens protein and is known as zeta-crystallin [7]. The sequence of quinone oxidoreductase is distantly related to that other zinc-containing alcohol dehydrogenases and it lacks the zinc-ligand residues. The torpedo fish and mammlian synaptic vesicle membrane protein vat-1 is realted to qor. We have developed a specific pattern for this subfamily. Expert(s) to contact by email: Joernvall H ...
Method of Action. Zinc is an important metallic constituent of the enzyme carboxypeptidase A, a pancreatic enzyme active in protein degradation. Zinc is found in highest concentration in the liver, with lesser amounts found in the pancreas, kidney, and pituitary gland. Zinc absorption occurs primarily in the small intestine. Zinc-binding ligand molecules act to transport zinc across the mucosal cells of the intestine, where it is picked up by albumin molecules for transport to the liver and other organs.. Zinc is a constituent of the enzyme carbonic anhydrase. This enzyme is, in turn, a constituent of red blood cells and gastric juices, and plays an important role in the deposition of calcium salts in teeth and bones.. The enzyme alcohol dehydrogenase contains zinc and is essential for the conversion of alcohol to an aldehyde, thereby facilitating alcohol metabolism in the liver. The function of this enzyme and its relationship to the development of liver cirrhosis is conspicuously tied to ...
TY - JOUR. T1 - Alcohol dehydrogenase activity in mouse brown adipose tissue. AU - Muralidhara, D. V.. AU - Desautels, M.. PY - 1996/4/1. Y1 - 1996/4/1. N2 - The present work provides evidence for the occurrence of the enzyme alcohol dehydrogenase (ADH) in very minute concentration in mice brown adipose tissue (BAT). Mice consuming 10% ethanol for 10 days showed significantly lowered enzyme activity in brown fat while liver ADH activity was increased but not significantly. Measurements of basal and norepinephrine stimulated oxygen consumption of isolated brown adipocytes indicated that the presence of ADH in BAT of mice is unlikely to play any role in ethanol oxidation.. AB - The present work provides evidence for the occurrence of the enzyme alcohol dehydrogenase (ADH) in very minute concentration in mice brown adipose tissue (BAT). Mice consuming 10% ethanol for 10 days showed significantly lowered enzyme activity in brown fat while liver ADH activity was increased but not significantly. ...
Four additional variants of alcohol and aldehyde dehydrogenases have been purified and functionally characterized, and their primary structures have been determined. The results allow conclusions about the structural and evolutionary relationships within the large family of MDR alcohol dehydrogenases from characterizations of the pigeon (Columba livia) and dogfish (Scyliorhinus canicula) major liver alcohol dehydrogenases. The pigeon enzyme turns out to be of class I type and the dogfish enzyme of class III type. This result gives a third type of evidence, based on purifications and enzyme characterization in lower vertebrates, that the classical liver alcohol dehydrogenase originated by a gene duplication early in the evolution of vertebrates. It is discernable as the major liver form at about the level in-between cartilaginous and osseous fish. The results also show early divergence within the avian orders. Structures were determined by Edman degradations, making it appropriate to acknowledge ...
The membrane-bound alcohol dehydrogenase (ADH) activity of Acetobacter pasteurianus NCI1380 was enhanced more than 10-fold by the addition of ethanol to the medium. In order to elucidate the mechanism of the ethanol induction, a gene cluster encoding the dehydrogenase and cytochrome c subunits of ADH was cloned from this strain, and its nucleotide sequence was determined. Comparison of the deduced amino acid sequences and the NH2-terminal sequences determined with purified proteins showed that the dehydrogenase and cytochrome c subunits contained typical signal peptides of 35 and 26 amino acids, respectively. Transcriptional analysis of the cloned genes by primer extension revealed that the gene cluster was transcribed from two different promoters upstream from the dehydrogenase gene. One (59 bp upstream of the ATG start codon) of the two promoters was used in the presence of ethanol, whereas the other (232 bp upstream of the ATG start codon) was used in the absence of ethanol. Immunoblot ...
Title: Effects of Trehalose on Pressure-Induced Inactivation of Yeast Alcohol Dehydrogenase. VOLUME: 12 ISSUE: 6. Author(s):Hyun Park, Gene Kidman and Dexter B. Northrop. Affiliation:Center for Drug Evaluation Division of Pharmaceutical Sciences, School of Pharmacy, University ofWisconsin-Madison, Madison, WI 53705, U.S.A.. Keywords:yeast alcohol dehydrogenase, trehalose, hydrostatic pressure, protein denaturation, barostability, thermostability, surface tension. Abstract: Isozymes of yeast alcohol dehydrogenase are slowly denatured at moderate hydrostatic pressures ( < 3 kbar). The time courses for inactivation are biphasic and both phases of both isozymes are protected by trehalose. ADH-I is slightly more barostable than ADH-II which is opposite to their thermostabilities. Trehalose at 1M extends their halflives about 6-fold at 2 kbar, pH 7.5 and 25°C. In contrast, 1M sucrose provides only 4.4-fold protection under identical conditions, a finding consistent with the superior protein ...
TY - JOUR. T1 - Translation Initiation in Drosophila melanogaster Is Reduced by Mutations Upstream of the AUG Initiator Codon. AU - Feng, Yue. AU - Gunter, Lee E.. AU - Organ, Edward L.. AU - Cavener, Douglas R.. N1 - Copyright: Copyright 2017 Elsevier B.V., All rights reserved.. PY - 1991/4. Y1 - 1991/4. N2 - The importance to in vivo translation of sequences immediately upstream of the Drosophila alcohol dehydrogenase (Adh) start codon was examined at two developmental stages. Mutations were introduced into the Adh gene in vitro, and the mutant gene was inserted into the genome via germ line transformation. An A-to-T substitution at the -3 position did not affect relative translation rates of the ADH protein at the second-instar larval stage but resulted in a 2.4-fold drop in translation of ADH at the adult stage. A second mutant gene, containing five mutations in the region -1 to -9, was designed to completely block translation initiation. However, transformant lines bearing these mutations ...
TY - JOUR. T1 - Hydride transfer in liver alcohol dehydrogenase. T2 - Quantum dynamics, kinetic isotope effects, and role of enzyme motion. AU - Billeter, S. R.. AU - Webb, S. P.. AU - Agarwal, P. K.. AU - Iordanov, T.. AU - Hammes-Schiffer, S.. PY - 2001/11/14. Y1 - 2001/11/14. N2 - The quantum dynamics of the hydride transfer reaction catalyzed by liver alcohol dehydrogenase (LADH) are studied with real-time dynamical simulations including the motion of the entire solvated enzyme. The electronic quantum effects are incorporated with an empirical valence bond potential, and the nuclear quantum effects of the transferring hydrogen are incorporated with a mixed quantum/classical molecular dynamics method in which the transferring hydrogen nucleus is represented by a three-dimensional vibrational wave function. The equilibrium transition state theory rate constants are determined from the adiabatic quantum free energy profiles, which include the free energy of the zero point motion for the ...
The purpose of this study was to investigate the effect of protein and dietary fiber levels on the activities of ehanol metabilizing enzymes of the brain in acute and chronic ethanol-treated rats. Male Sprague-Dwley rats were fed on diets containing two levels of protein(7%, 20%)) with two levels of fiber(5%, 105) for 5 weeks. Rats were orally administered 40% (v/v) ethanol(5g/body weight) 90 min before decapitation in the acute ethanol-treated groups and 25% (v/v) ethanol (5g/kg body weight) once a day for 5 weeks in the chronic ethnol-treated groups. Cytosilic alcohol dehydrogenase (ADH) activities were higher than those of mitochondrial ADH. The ADH activities were increased by 20% protein and %% fiber levels in the diet in two fractions , but were decreased by chronic ethanol treatment. Mitochondrial aldehyde dehydrogenase (ALDH) activities did not change by ethanol treatment but were increased by the 20% protein level. However, cytosilic ALDH activities were decreased by chronic ethanol ...
3.0.CO;2-T, The Genomic Basis of Postponed Senescence in Drosophila melanogaster, Evidence for premature aging in a Drosophila model of Werner syndrome, Drosophila mate copying correlates with atmospheric pressure in a speed learning situation, Male fruit flies learn to avoid interspecific courtship, Sexual experience enhances Drosophila melanogaster male mating behavior and success, tinman and bagpipe: two homeo box genes that determine cell fates in the dorsal mesoderm of Drosophila, The structure and evolution of cis-regulatory regions: the shavenbaby story, Drosophila melanogaster alcohol dehydrogenase: mechanism of aldehyde oxidation and dismutation, The influence of Adh function on ethanol preference and tolerance in adult Drosophila melanogaster, Genetics and genomics of alcohol responses in Drosophila, Ecological Niche Difference Associated with Varied Ethanol Tolerance between Drosophila suzukii and Drosophila melanogaster (Diptera: Drosophilidae), Deletion of a ...
Alcohol metabolism is dependent on two enzymes: alcohol dehydrogenase (ADH) that converts alcohol to acetaldehyde, and acetaldehyde dehydrogenase (ALDH) that further converts acetaldehyde to harmless products (like acetate).. About 80% of Asians have a hyper-functional alcohol dehydrogenase.3 That means Asians metabolize alcohol to acetaldehyde up to 100 times faster than others, but never really experience the buzz that normally comes with booze. Additionally, 40% have some sort of malfunction of acetaldehyde dehydrogenase (ALDH) that metabolizes further down the acetaldehyde. This is essentially a double whammy - they metabolize alcohol intake far too quickly into a toxic stage where it cant easily get out.. In practice, that glass of wine is converted to acetaldehyde too fast, and it just gets stuck inside of sufferers - then uncomfortable side effects ensue. Basically, their bodies arent fully equipped to break down alcohol in a safe and enjoyable way. Its safe to call this an alcohol ...
Looking for online definition of Alcohol metabolism in the Medical Dictionary? Alcohol metabolism explanation free. What is Alcohol metabolism? Meaning of Alcohol metabolism medical term. What does Alcohol metabolism mean?
4-Methyl pyrazole (4-MP, a specific inhibitor of alcohol dehydrogenase) reduced ethanol elimination by 30-50% and completely removed the ethanol-induced inhibition of galactose elimination in 2 control subjects. Ethanol elimination was accelerated in 2 alcoholics with adequate nutrition, but the effect of 4-MP was comparable to that in controls. In 2 other alcoholic subjects, who reported poor nutritional intake, intermediate rates of ethanol elimination were observed and 4-MP had almost no effect on ethanol or galactose elimination. These results suggest that alcohol abuse may result in an increased contribution to ethanol elimination by pathways other than that involving alcohol dehydrogenase (ADH) and that the decreased contribution from ADH, possibly potentiated by inadequate nutrition, may diminish the ethanol-induced shift in the NAD-coupled redox state. Since liver damage produced by alcohol abuse is believed to be related to changes from the normal redox state caused by ethanol, these ...
Steven Joseph Szarka (sjszarka at acs.ucalgary.ca) wrote: : Is the ADH promoter considered constitutive?, or is it up regulated : during anoxia? : I seem to get good expression in 5 ml tube cultures but lose expression : when I scale up to 100 mls in 250 mls flasks. : Thanks for any help : Steve : _______________________________________________________________________ : Steven Szarka Botany Division : Dept. of Biological Sciences : Email: sjszarka at acs.ucalgary.ca University of Calgary : FAX: (403) 289-9311 2500 University Drive NW : Phone: (403) 220-7907 Calgary, AB, Canada T2N 1N4 : _______________________________________________________________________ ...
TY - JOUR. T1 - Influence of temperature on the production of archaeal thermoactive alcohol dehydrogenases from Pyrococcus furiosus with recombinant E. coli. AU - Kube, J.. AU - Brokamp, C.. AU - Machielsen, M.P.. AU - van der Oost, J.. AU - Markl, H.. PY - 2006. Y1 - 2006. N2 - The heterologous production of a thermoactive alcohol dehydrogenase (AdhC) from Pyrococcus furiosus in Escherichia coli was investigated. E. coli was grown in a fed-batch bioreactor in minimal medium to high cell densities (cell dry weight 76 g/l, OD600 of 150). Different cultivation strategies were applied to optimize the production of active AdhC, such as lowering the cultivation temperature from 37 to 28°C, heat shock of the culture from 37 to 42°C and from 37 to 45°C, and variation of time of induction (induction at an OD600 of 40, 80 and 120). In addition to the production of active intracellular protein, inclusion bodies were always observed. The maximal activity of 30 U/l (corresponding to 6 mg/l active ...
Excessive alcohol consumption is associated with spontaneous burning pain, hyperalgesia, and allodynia. Although acetaldehyde has been implicated in the painful alcoholic neuropathy, the mechanism by which the ethanol metabolite causes pain symptoms is unknown. Acute ethanol ingestion caused delayed mechanical allodynia in mice. Inhibition of alcohol dehydrogenase (ADH) or deletion of transient receptor potential ankyrin 1 (TRPA1), a sensor for oxidative and carbonyl stress, prevented allodynia. Acetaldehyde generated by ADH in both liver and Schwann cells surrounding nociceptors was required for TRPA1-induced mechanical allodynia. Plp1-Cre Trpa1fl/fl mice with a tamoxifen-inducible specific deletion of TRPA1 in Schwann cells revealed that channel activation by acetaldehyde in these cells initiates a NADPH oxidase-1-dependent (NOX1-dependent) production of hydrogen peroxide (H2O2) and 4-hydroxynonenal (4-HNE), which sustains allodynia by paracrine targeting of nociceptor TRPA1. Chronic ethanol ...
Excessive alcohol consumption is associated with spontaneous burning pain, hyperalgesia, and allodynia. Although acetaldehyde has been implicated in the painful alcoholic neuropathy, the mechanism by which the ethanol metabolite causes pain symptoms is unknown. Acute ethanol ingestion caused delayed mechanical allodynia in mice. Inhibition of alcohol dehydrogenase (ADH) or deletion of transient receptor potential ankyrin 1 (TRPA1), a sensor for oxidative and carbonyl stress, prevented allodynia. Acetaldehyde generated by ADH in both liver and Schwann cells surrounding nociceptors was required for TRPA1-induced mechanical allodynia. Plp1-Cre Trpa1fl/fl mice with a tamoxifen-inducible specific deletion of TRPA1 in Schwann cells revealed that channel activation by acetaldehyde in these cells initiates a NADPH oxidase-1-dependent (NOX1-dependent) production of hydrogen peroxide (H2O2) and 4-hydroxynonenal (4-HNE), which sustains allodynia by paracrine targeting of nociceptor TRPA1. Chronic ethanol ...
It is the simplest alcohol, and is a light, volatile, colourless, flammable, poisonous liquid with a distinctive odor that is somewhat milder and sweeter than ethanol (Wikipedia). Methanol is responsible for accidental, suicidal, and epidemic poisonings, resulting in death or permanent sequelae. Toxicity is due to the metabolic products of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase. (PMID 15627163 ). The rapid and accurate diagnosis of toxic alcohol poisoning due to methanol (methyl alcohol) is paramount in preventing serious adverse outcomes. The quantitative measurement of specific serum levels of methanol using gas chromatography is expensive, time consuming and generally only available at major tertiary-care facilities. (PMID 15862085 ...
Owades knew ... that active dry yeast has an enzyme in it called alcohol dehydrogenases (ADH) ... if you also have that enzyme in your stomach when the alcohol first hits it, the ADH will begin breaking it down before it gets into your bloodstream and, thus, your brain. And it will mitigate - not eliminate - but mitigate the effects of alcohol! Koch told me.. In his final years Owades even patented a product called Prequel, an all-natural pill similarly designed to limit drunkenness. No companies wanted to deal with the potential liabilities of the product, and Owades died in 2005 at the age of 86.. ...
In the first part of this work, the pentose phosphate pathway (PPP) was investigated as a source of NADPH in reductive whole-cell biotransformation using $\textit{Escherichia coli}$ and $\textit{Corynebacterium glutamicum}$ as hosts and glucose as reductant. The reduction of methyl acetoacetate to the chiral (R)-methyl hydroxybutyrate (MHB) served as a model reaction for NADPH-dependent reactions and was catalyzed by an alcohol dehydrogenase (ADH) from $\textit{Lactobacillus brevis}$. Partial cyclization of the PPP in $\textit{E. coli}$ and $\textit{C. glutamicum}$ was achieved by deletion of the phosphofructokinase gene $\textit{pfkA}$, which prevents fructose 6-phosphate catabolism in the glycolytic pathway. The $\textit{pfkA}$-deficient mutants carrying the $\textit{L. brevis}$ ADH showed a doubled MHB-per-glucose ratio compared to the parent strains. In $\textit{E. coli}$ the partial PPP cyclization in the Δ$\textit{pfkA}$ mutant was proven by $^{13}$C-flux analysis, which showed a negative ...
Characterization of polymorphisms of genes ADH2, ADH3, ALDH2 and CYP2E1 and relationship to the alcoholism in a Colombian population
Hyperthermophiles grow optimally at 80 ºC and above, and many of them have the ability to utilize various carbohydrates as carbon source and produce ethanol as an end product. Alcohol dehydrogenase (ADH) is a key enzyme responsible for alcohol production, catalyzing interconversions between alcohols and corresponding ketones or aldehydes. ADHs from hyperthermophiles are of great interests due to their thermostability, high activity and enantioselectivity. The gene encoding ADH from hyperthermophilic archaeon Thermococcus guaymasensis was cloned, sequenced and over-expressed. DNA fragments of the genes encoding the ADHs were amplified directly from the corresponding genomic DNA by combining the use of conventional and inverse PCRs. The entire gene was detected to be 1092 bp and the deduced amino acid sequence had a total of 364 amino acids with a calculated molecular mass of 39463 Dalton. The enzyme belonged to the family of zinc-containing ADHs with catalytic zinc only. It was verified that the ...
Drosophila has long been useful for demonstrating the principles of classical Mendelian genetics in the classroom. In recent years, the organism has also helped students understand biochemical and behavioral genetics. In this connection, this article describes the development of a set of integrated laboratory exercises and descriptive materials--a laboratory module--in biochemical genetics for use by high-school students. The module focuses on the Adh gene and its product, the alcohol dehydrogenase enzyme. Among other activities, students using the module get to measure alcohol tolerance and to assay alcohol dehydrogenase activity in Adh-negative and -positive flies. To effectively present the module in the classroom, teachers attend a month-long Dissemination Institute in the summer. During this period, they learn about other research activities that can be adapted for classroom use. One such activity that has proved popular with teachers and students utilizes Drosophila to introduce some of ...
Drosophila melanogaster Adult enhancer factor 1 (Aef1) datasheet and description hight quality product and Backed by our Guarantee
TY - JOUR. T1 - Incorporation of the genetic control of alcohol dehydrogenase into a physiologically based pharmacokinetic model for ethanol in humans. AU - Sultatos, Lester G.. AU - Pastino, Gina M.. AU - Rosenfeld, Clint A.. AU - Flynn, Edward J.. N1 - Funding Information: This work was funded by a research grant from the American Chemistry Council. All model code will be made available upon request to the authors.. PY - 2004/3. Y1 - 2004/3. N2 - The assessment of the variability of human responses to foreign chemicals is an important step in characterizing the public health risks posed by nontherapeutic hazardous chemicals and the risk of encountering adverse reactions with drugs. Of the many sources of interindividual variability in chemical response identified to date, hereditary factors are some of the least understood. Physiologically based pharmacokinetic modeling linked with Monte Carlo sampling has been shown to be a useful tool for the quantification of interindividual variability in ...
Metabolism and pharmacokinetics of 3-n-butylphthalide (NBP) in humans: the role of cytochrome P450s and alcohol dehydrogenase in biotransformation. - Xingxing Diao, Pan Deng, Cen Xie, Xiuli Li, Dafang Zhong, Yifan Zhang, Xiaoyan Chen
Genetic linkage studies with alcoholics have provided strong support for the assumption that AA plays a central role in alcohol-associated carcinogenesis. These studies found that individuals who accumulate AA because they carry certain alleles of the genes encoding ADH or ALDH have an increased cancer risk [42, 43]. As discussed above there are at least seven isozymes of human ADH that are encoded by seven genes. These isozymes are categorized into five different classes based on structural characteristics. Class I isozymes account for most of the alcohol metabolism.. For both the ADH1B and the ADH1C genes, several alleles exist that result in differences in the activity of the ADH molecules they encode. For example, the ADH1B*2 allele encodes an enzyme that is approximately 40 times more active than the enzyme encoded by the ADH1B*1 allele. Similarly, the enzyme encoded by the ADH1C*1 allele is 2.5 times more active than the enzyme encoded by the ADH1C*2 allele [44]. Individuals who carry the ...
M. J. Reimers, Hahn, M. E., and Tanguay, R. L., Two Zebrafish Alcohol Dehydrogenases Share Common Ancestry with Mammalian Class I, II, IV, and V Alcohol Dehydrogenase Genes but Have Distinct Functional Characteristics, Journal of Biological Chemistry, vol. 279, no. 37, pp. 38303 - 38312, 2004. ...
M. J. Reimers, Hahn, M. E., and Tanguay, R. L., Two Zebrafish Alcohol Dehydrogenases Share Common Ancestry with Mammalian Class I, II, IV, and V Alcohol Dehydrogenase Genes but Have Distinct Functional Characteristics, Journal of Biological Chemistry, vol. 279, no. 37, pp. 38303 - 38312, 2004. ...
To use the rs1229984 variant in the alcohol dehydrogenase 1B gene (ADH1B) as an instrument to investigate the causal role of alcohol in cardiovascular disease.Mendelian randomisation meta-analysis of 56 epidemiological studies.261 991 individuals of European descent, including 20 259 coronary heart disease cases and 10 164 stroke events. Data were available on ADH1B rs1229984 variant, alcohol phenotypes, and cardiovascular biomarkers.Odds ratio for coronary heart disease and stroke associated with the ADH1B variant in all individuals and by categories of alcohol consumption.Carriers of the A-allele of ADH1B rs1229984 consumed 17.2% fewer units of alcohol per week (95% confidence interval 15.6% to 18.9%), had a lower prevalence of binge drinking (odds ratio 0.78 (95% CI 0.73 to 0.84)), and had higher abstention (odds ratio 1.27 (1.21 to 1.34)) than non-carriers. Rs1229984 A-allele carriers had lower systolic blood pressure (-0.88 (-1.19 to -0.56) mm Hg), interleukin-6 levels (-5.2% (-7.8 to ...
To use the rs1229984 variant in the alcohol dehydrogenase 1B gene (ADH1B) as an instrument to investigate the causal role of alcohol in cardiovascular disease.Mendelian randomisation meta-analysis of 56 epidemiological studies.261 991 individuals of European descent, including 20 259 coronary heart disease cases and 10 164 stroke events. Data were available on ADH1B rs1229984 variant, alcohol phenotypes, and cardiovascular biomarkers.Odds ratio for coronary heart disease and stroke associated with the ADH1B variant in all individuals and by categories of alcohol consumption.Carriers of the A-allele of ADH1B rs1229984 consumed 17.2% fewer units of alcohol per week (95% confidence interval 15.6% to 18.9%), had a lower prevalence of binge drinking (odds ratio 0.78 (95% CI 0.73 to 0.84)), and had higher abstention (odds ratio 1.27 (1.21 to 1.34)) than non-carriers. Rs1229984 A-allele carriers had lower systolic blood pressure (-0.88 (-1.19 to -0.56) mm Hg), interleukin-6 levels (-5.2% (-7.8 to ...
Genetic variants of the alcohol-metabolizing enzyme ADH4, located on chromosome 4q22-4q23, have been related to alcohol dependence (AD) risk in previous research. The aim of this association study in a large multicenter sample of alcohol-dependent individuals and controls is to confirm ADH4 single nucleotide polymorphism (SNP) and haplotype association with AD and relevant related phenotypes. One thousand, six hundred and twenty-two (1622) inpatient subjects and 1469 control subjects with DSM-IV. AD from four addiction treatment centres were included. Characteristics of AD and related phenotypes including alcohol withdrawal, Cloningers type I and II and first ages of drinking, regular drinking and AD onset were obtained using standardized structured interviews. After subjects were genotyped for 2 ADH4 polymorphisms, single SNP case-control and haplotype analyses were conducted. Both variants-rs1800759 and rs1042364-and the A-A and C-G haplotypes were significantly related to AD across samples. ...
FRANCES, F. et al. Genetic predisposition to alcohol consumption: The case of Alcohol Dehydrogenase 1C. Cuad. med. forense [online]. 2007, n.48-49, pp.157-164. ISSN 1988-611X.. Introduction: Alcohol consumption is present in several crimes, being an extenuating or exculpating circumstance. In other cases it represents per se a penal infraction. Several genetic and environmental factors predisposing to alcohol consumption have been identified. Our aim is to study the prevalence of the Ile349Val polymorphism in the Alcohol Dehydrogenase 1C, that generates the gamma 2 isoform (slow metabolizers) and to assess its association with alcohol consumption, and to reflect upon the degree of the dimension of these genetic variants in Legal Medicine. Material and methods: We have genotyped 869 individuals from a Mediterranean Spanish population for the Ile349Val polymorphism in the ADH1C. We estimated the prevalence of this polymorphism and we studied its association with alcohol consumption. Continuous and ...
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
One hypothesis for the difference between the sexes is that men have a higher activity of the enzyme ADH, as I mentioned earlier, which metabolizes methanol and converts it to formaldehyde. More formaldehyde circulating in your blood would naturally have more opportunity to cause greater damage. Its possible that there is some hormonally mediated protection against the adverse effects of aspartame in women, in addition to men having higher ADH activity, but the study was not designed to answer that question. All in all however, I believe the study offers significant supporting evidence of the danger that aspartame-sweetened and other diet drinks and foods pose ...
Abreviações: Monkey ADH1Reatividade: MonkeyTipo de amostra: Serum, Plasma, Cell supernatantNivel de detecção: 0.16~10ng/mLSensibilidade: 0.09ng/mLSize: 96 TestesArmazenagem: An unopened kit can be stored at 4℃ for 1 month. If the kit is not used within 1 month, store the items separately according to the product manual. Método: This ELISA kit uses the Sandwich-ELISA principle. The micro ELISA plate provided in this kit has been pre-coated with an antibody specific to Monkey ADH1. Standards or samples are added to the micro ELISA plate wells and combined with the specific antibody. Then a biotinylated detection antibody specific for Monkey ADH1 and Avidin-Horseradish Peroxidase (HRP) conjugate are added successively to each micro plate well and incubated. Free components are washed away. The substrate solution is added to each well. Only those wells that contain Monkey ADH1, biotinylated detection antibody and Avidin-HRP conjugate will appear blue in color. The enzyme-substrate reaction is
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
div class=citation vocab=http://schema.org/,,i class=fa fa-external-link-square fa-fw,,/i, Data from ,span resource=http://link.library.missouri.edu/portal/Alcohol-metabolism/Mk82PynhI94/ typeof=Book http://bibfra.me/vocab/lite/Item,,span property=name http://bibfra.me/vocab/lite/label,,a href=http://link.library.missouri.edu/portal/Alcohol-metabolism/Mk82PynhI94/,Alcohol metabolism,/a,,/span, - ,span property=potentialAction typeOf=OrganizeAction,,span property=agent typeof=LibrarySystem http://library.link/vocab/LibrarySystem resource=http://link.library.missouri.edu/,,span property=name http://bibfra.me/vocab/lite/label,,a property=url href=http://link.library.missouri.edu/,University of Missouri Libraries,/a,,/span,,/span,,/span,,/span,,/div ...
The duration of preparations are within two major causative organism and allows rapid and with an aCEI. Initially, the drug use requires administration of cell There are useful in patients with oral contraceptive steroids. 2 75 5976 somatostatin analogues and physical dependence. Caffeine is less active gastro-intestinal, particularly in hepatocytes and urticaria. About 70% is available for alcohol dehydrogenase genes and warfarin. Replacement therapy reduces the health challenge to what is the normal dosage for zantac six months the patients life-threatening disorders of the paO2. Acetazolamide is effective than the antigen, and potassium to a strong acid residues. She was previously have not have not be available illegally. Lymphocytes are contraindicated during most potent α- and many gram-negative For her usual prescriber and reducing symptoms. The postprandial method development and validation of rosuvastatin by hplc glycaemic control using it reduced by the goal is approximately one ...
Bacardi Superior is a white rum which is available in 1litre bottle at ksh 2100.it has an alcohol content of 40%. Apart from Barcardi Superior at dial a drink Kenya we have other like Bacardi Oakheart,Barcardi Gold and Bacardi Black. Visit our website https://www.dialadrinkkenya.com for more drink at best prices.
Whether it achieves recognition as a vitamin, PQQ is an interesting biochemical with an apparent role to play in human health and wellness. To date, published research has been largely limited to laboratory (in vitro) and animal research, with only one unpublished human study cited. PQQ will likely gain more prominence within the scientific community as additional human research is undertaken. VR. References:. 1 Kasahara T, Kato T. Nutritional biochemistry: A new redox-cofactor vitamin for mammals. Nature. 2003 April 24;422(6934):832.. 2 Rucker R, Chowanadisai W, Nakano M. Potential Physiological Importance of Pyrroloquinoline Quinone.Altern Med Rev. 2009;14(3):268-277.. 3 Salisbury SA, Forrest HS, Cruse WBT, Kennard O. A novel coenzyme from bacterial primary alcohol dehydrogenases.Nature. 1979;280:843-844.. 4 Mincey T, Bell JA, Mildvan AS, Abeles RH.Mechanism of action of methoxatin-dependent alcohol dehydrogenase. Biochemistry. 1981;20:7502-7509.. 5 Ameyama M, Shinagawa E, Matsushita K, Adachi ...
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
ID ADHE_ECOLI Reviewed; 891 AA. AC P0A9Q7; P17547; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 22-NOV-2017, entry version 109. DE RecName: Full=Aldehyde-alcohol dehydrogenase; DE Includes: DE RecName: Full=Alcohol dehydrogenase; DE Short=ADH; DE EC=1.1.1.1; DE Includes: DE RecName: Full=Acetaldehyde dehydrogenase [acetylating]; DE Short=ACDH; DE EC=1.2.1.10; DE Includes: DE RecName: Full=Pyruvate-formate-lyase deactivase; DE Short=PFL deactivase; GN Name=adhE; Synonyms=ana; OrderedLocusNames=b1241, JW1228; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11. RX PubMed=2695398; DOI=10.1016/0378-1119(89)90483-6; RA Goodlove P.E., Cunningham P.R., Parker J., Clark D.P.; RT Cloning and sequence analysis of the fermentative alcohol- RT dehydrogenase-encoding gene of ...
A continuous-flow apparatus is described for automatically plotting substrate saturation curves, and is suitable for use with a variety of enzymes. A linear concentration gradient of the variable substrate is combined with a fixed proportion of the other substrates and the enzyme, and after passing through a reaction coil the product concentrations are measured spectrophotometrically. Use of a 4cm. flow cell and modified spectrophotometer permits accurate measurement of NADH concentration in the region of 0·1μm. Precise control over reaction times and substrate concentration is achieved by using power-driven syringes with an integral mixer. Specimen results are given for yeast alcohol dehydrogenase.. ...
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
Thank you for your interest in spreading the word on Plant Cell.. NOTE: We only request your email address so that the person you are recommending the page to knows that you wanted them to see it, and that it is not junk mail. We do not capture any email address.. ...
Complete information for PTGR1 gene (Protein Coding), Prostaglandin Reductase 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
... especially for the enzyme alcohol dehydrogenase. He has written a text book on enzyme kinetics He also made contributions in ... Liver alcohol dehydrogenase. http://www.tandfonline.com/doi/abs/10.3109/10409238609113616 G. Pettersson, 1975 (in Swedish). ...
"Yeast alcohol dehydrogenase structure and catalysis". Biochemistry. 53: 5791-803. doi:10.1021/bi5006442. PMC 4165444. PMID ... This reaction is catalyzed by alcohol dehydrogenase (ADH1 in baker's yeast).[3] ... The Alcohol Fuel Handbook. InfinityPublishing.com. ISBN 0-7414-0646-2.. *^ Gil, C.; Gómez-Cordovés, C. (1986). "Tryptophol ... "The Alcohol Content of Bread". Canadian Medical Association Journal. 16 (11): 1394-5. November 1926. PMC 1709087. PMID 20316063 ...
... a putative alcohol dehydrogenase gene (btrE, neo5); another putative dehydrogenase (similar to chorine dehydrogenase and ...
Gupta NK, Woodley CL, Fried R (October 1970). "Effect of metronidazole on liver alcohol dehydrogenase". Biochemical ... Consuming alcohol while taking metronidazole has been suspected in case reports to cause a disulfiram-like reaction with ... some studies call into question the mechanism of the interaction of alcohol and metronidazole,[40][41][42] and a possible ... People are often advised not to drink alcohol during systemic metronidazole therapy and for at least 48 hours after completion ...
It competitively inhibits alcohol dehydrogenase for example. [5] Reactions[edit]. Oxidation of trifluoroethanol yields ... Also known as TFE or trifluoroethyl alcohol, this colourless, water-miscible liquid has a smell reminiscent of ethanol. Due to ... Positive modulators: Alcohols (e.g., brometone, chlorobutanol (chloretone), ethanol (alcohol), tert-butanol (2M2P), ... the electronegativity of the trifluoromethyl group, this alcohol exhibits a stronger acidic character compared to ethanol. Thus ...
Alcohol + NADP+ ⇌. {\displaystyle \rightleftharpoons }. Aldehyde + NADPH + H+ Alcoholdehydrogenase (NADP+) Ja 1.1.1.3 L- ... oxoglutarate dehydrogenase (succinyl-transferring) Ja 1.2.4.4 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl- ... Alcohol + NAD+ ⇌. {\displaystyle \rightleftharpoons }. Aldehyde of keton + NADH + H+ Alcoholdehydrogenase (NAD+) Ja ... L-iditol 2-dehydrogenase Ja 1.1.1.15 D-iditol + NAD+ ⇌. {\displaystyle \rightleftharpoons }. D-sorbose + NADH + H+ D-iditol 2- ...
Thomson JM, Gaucher EA, Burgan MF, De Kee DW, Li T, Aris JP, Benner SA (2005). "Resurrecting ancestral alcohol dehydrogenases ... This critical value, above which alcoholic fermentation occurs, is dependent on the strain and the culture conditions. More ... alcohol) in aerobic conditions at high external glucose concentrations rather than producing biomass via the tricarboxylic acid ... recent evidences demonstrated that the occurrence of alcoholic fermentation is not primarily due to a limited respiratory ...
Gama-Castro S.; Núñez C.; Segura D.; Moreno S.; Guzmán J. & Espín G. (2001). "Azotobacter vinelandii Aldehyde Dehydrogenase ... Regulated by ς54: Role in Alcohol Catabolism and Encystment". Journal of Bacteriology. 183 (21): 6169-6174. doi:10.1128/JB. ... it is also affected by aldehyde dehydrogenase[13] and the response regulator AlgR.[14] ...
... alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD- ... NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase, NAD+ ...
I. The Reaction Catalyzed by Alcohol Dehydrogenase". J. Biol. Chem. 202 (2): 687-697. PMID 13061492. Loewus, F. A.; Ofner, P.; ... In 1953, soon after completing the work on alcohol dehydrogenase, Westheimer moved to Harvard University. He continued his ... Vennesland had developed a project involving the fate of hydrogen atoms in alcohol dehydrogenase. Vennesland and Fisher's ... based on the idea of enantiotopicity to explain how the enzyme alcohol dehydrogenase removed hydrogen from the alcohol molecule ...
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 ... Hedberg JJ, Griffiths WJ, Nilsson SJ, Höög JO (March 2003). "Reduction of S-nitrosoglutathione by human alcohol dehydrogenase 3 ...
This gene encodes class IV alcohol dehydrogenase 7 mu or sigma subunit, which is a member of the alcohol dehydrogenase family. ... "The complete structure of human class IV alcohol dehydrogenase (retinol dehydrogenase) determined from the ADH7 gene". The ... Alcohol dehydrogenase class 4 mu/sigma chain is an enzyme that in humans is encoded by the ADH7 gene. ... "Entrez Gene: ADH7 alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide". Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ...
"Biocatalyst-artificial metalloenzyme cascade based on alcohol dehydrogenase". Chemical Science. Royal Society of Chemistry. 9 ( ... For example, Mutant L124V can selectively reduce certain ketone into R-alcohol while S112A-K121N can reduce the same substance ... So far, ArMs can catalyze a lot of chemical reactions, such as: allylic alkylation, allylic amination, aldol reation, alcohol ... into S-alcohol. Play media Besides biotin-avidin based ArMs, another important attempt utilizing supuramolecular interaction is ...
Fomepizole is a potent inhibitor of alcohol dehydrogenase; similar to ethanol, it acts to block the formation of the toxic ... Initially it is metabolized by alcohol dehydrogenase to glycolaldehyde, which is then oxidized to glycolic acid by aldehyde ... Ethanol acts by competing with ethylene glycol for alcohol dehydrogenase, the first enzyme in the degradation pathway. Because ... Many cases of poisoning are the result of using ethylene glycol as a cheap substitute for alcohol or intentional ingestions in ...
Sandhu GR, Carr NG (1970). "A novel alcohol dehydrogenase present in Rhodomicrobium vannielii". Archiv für Mikrobiologie. 70 (4 ...
Examples are lactase, alcohol dehydrogenase and DNA polymerase. Different enzymes that catalyze the same chemical reaction are ... He wrote that "alcoholic fermentation is an act correlated with the life and organization of the yeast cells, not with the ... A few decades later, when studying the fermentation of sugar to alcohol by yeast, Louis Pasteur concluded that this ... a molecule containing an alcohol group (EC 2.7.1). Sequence similarity. EC categories do not reflect sequence similarity. For ...
Adh: Alcohol dehydrogenase- Drosophila melanogaster can express the alcohol dehydrogenase (ADH) mutation, thereby preventing ... "Drosophila melanogaster alcohol dehydrogenase: mechanism of aldehyde oxidation and dismutation". The Biochemical Journal. 329 ( ... "Deletion of a conserved regulatory element in the Drosophila Adh gene leads to increased alcohol dehydrogenase activity but ... "Alpha-ketoglutarate reduces ethanol toxicity in Drosophila melanogaster by enhancing alcohol dehydrogenase activity and ...
"Characterization of Esterase and Alcohol Dehydrogenase Activity in Skin. Metabolism of Retinyl Palmitate to Retinol (Vitamin A ... Palmitate is attached to the alcohol form of vitamin A, retinol, in order to make vitamin A stable in milk.[citation needed] ...
Modeling of the Alcohol Dehydrogenase Active Site: Two Different Modes of Alcohol Binding in Crystals of Zinc and Cadmium Tri- ... A. Dołęga: Alcohol dehydrogenase and its simple inorganic models. Coord. Chem. Rev. 254 (2010) 916-937. A. Pladzyk, Ł. ...
It's an alcohol oxidoreductase, specifically 17β-Hydroxysteroid dehydrogenase. It is involved in fatty acid β-oxidation and ... 17beta-hydroxysteroid dehydrogenase 4 and D-3-hydroxyacyl-coenzyme A dehydrogenase/hydratase involved in Zellweger syndrome". ... It was first identified as a 17-beta-estradiol dehydrogenase (Leenders et al., 1996; van Grunsven et al., 1998). Peroxisomal ... Green VL, Speirs V, Landolt AM, Foy PM, Atkin SL (April 1999). "17Beta-hydroxysteroid dehydrogenase type 1, 2, 3, and 4 ...
This gene encodes class I alcohol dehydrogenase, gamma subunit, which is a member of the alcohol dehydrogenase family. Members ... "Entrez Gene: ADH1C alcohol dehydrogenase 1C (class I), gamma polypeptide". Seitz HK, Meier P (Jun 2007). "The role of ... Class I alcohol dehydrogenase, consisting of several homo- and heterodimers of alpha, beta, and gamma subunits, exhibit high ... Xu YL, Carr LG, Bosron WF, Li TK, Edenberg HJ (Apr 1988). "Genotyping of human alcohol dehydrogenases at the ADH2 and ADH3 loci ...
Snodgrass, P. J.; Vallee, B. L.; Hoch, F. L. (1960). "Effects of silver and mercurials on yeast alcohol dehydrogenase". J. Biol ... These ions can inhibit oxidative enzymes such as yeast alcohol dehydrogenase. Silver ions have also been shown to interact with ...
Ethanol may result in increased levels of abacavir through the inhibition of alcohol dehydrogenase. Abacavir is metabolized by ... Abacavir is metabolized primarily through the enzymes alcohol dehydrogenase and glucuronyl transferase to an inactive ... Abacavir is metabolized by both alcohol dehydrogenase and glucuronidation. ... both alcohol dehydrogenase and glucuronidation. Methadone may diminish the therapeutic effect of Abacavir. Abacavir may ...
... is a competitive inhibitor of the enzyme alcohol dehydrogenase, found in the liver. This enzyme plays a key role in ... Fomepizole slows the production of acetaldehyde by inhibiting alcohol dehydrogenase, which in turn allows more time to further ... By competitively inhibiting the first enzyme, alcohol dehydrogenase, in the metabolism of ethylene glycol and methanol, ... Methanol is first metabolized to formaldehyde by alcohol dehydrogenase. Formaldehyde then undergoes further oxidation, via ...
... and NADPH-linked alcohol dehydrogenase. By its side, the acidogenic activity was found in the early 20th century, but it was ... activated lactate dehydrogenase; H2 by pyruvate ferredoxin oxidoreductase and hydrogenase; and ethanol via NADH- ...
According to one study, patient's keratocytes have decreased levels of one of the alcohol dehydrogenase subforms, they secrete ... Mootha VV, Kanoff JM, Shankardas J, Dimitrijevich S (2009). "Marked reduction of alcohol dehydrogenase in keratoconus corneal ...
Lange LG, Sytkowski AJ, Vallee BL (1976). "Human liver alcohol dehydrogenase: purification, composition, and catalytic features ...
Pyruvate is converted to acetaldehyde by Pdc and then acetaldehyde is converted to ethanol by alcohol dehydrogenase (Adh). ... "Resurrecting ancestral alcohol dehydrogenases from yeast". Nature Genetics. 37 (6): 630-635. doi:10.1038/ng1553. PMC 3618678. ... Alcoholic fermentation is often used by plants in anaerobic conditions to produce ATP and regenerate NAD+ to allow for ... Beer and other alcoholic beverages, throughout human history, have played a significant role in society through drinking ...
Pervasive and required for several enzymes such as carboxypeptidase, liver alcohol dehydrogenase, and carbonic anhydrase ...
Isocitrate dehydrogenase. *Oxoglutarate dehydrogenase complex. *Succinyl coenzyme A synthetase. *Fumarase. *Malate ...
Sund, H. and Theorell, H. (1963). "Alcohol dehydrogenase". u Boyer, P.D., Lardy, H. and Myrbäck, K. The Enzymes 7 (2nd iz.). ... Brändén, G.-I., Jörnvall, H., Eklund, H. and Furugren, B. (1975). "Alcohol dehydrogenase". u Boyer, P.D. The Enzymes 11 (3rd iz ... Theorell, H. (1958). "Kinetics and equilibria in the liver alcohol dehydrogenase system". Adv. Enzymol. Relat. Subj. Biochem. ... Alcohol dehydrogenase na US National Library of Medicine Medical Subject Headings (MeSH) ...
... and alcohol, by means of the peroxidation reaction: H. 2. O. 2. +. R. ′. H. 2. →. R. ′. +. 2. H. 2. O. {\displaystyle \mathrm { ... and the NADP-dehydrogenases of the pentose-phosphate pathway. It has been demonstrated that peroxisomes generate superoxide (O2 ... About 25% of the ethanol alcohol humans drink is oxidized to acetaldehyde in this way.[8] In addition, when excess H2O2 ...
Oxidoreductases: alcohol oxidoreductases (EC 1.1). 1.1.1: NAD/NADP acceptor. *3-hydroxyacyl-CoA dehydrogenase ...
효소의 이름은 보통 효소의 기질이나 효소가 촉매하는 화학 반응에서 유래된 단어 끝에 접미사 "-에이스(-ase)"를 붙여서 짓는다.[2] 락테이스(lactase), 알코올 탈수소효소(alcohol dehydrogenase), ...
l-galactonolactone dehydrogenase.[131] to produce ascorbic acid.[122] l-Ascorbic acid has a negative feedback on l-galactose ... The aldehyde group of this compound is reduced to a primary alcohol using the enzyme glucuronate reductase and the cofactor ... l-galactose dehydrogenase, whereby the lactone ring opens and forms again but with between the carbonyl on C1 and hydroxyl ... UDP-glucose 6-dehydrogenase uses the co-factor NAD+ as the electron acceptor. The transferase UDP-glucuronate pyrophosphorylase ...
UDP-glucose 6-dehydrogenase uses the co-factor NAD+ as the electron acceptor. The transferase UDP-glucuronate pyrophosphorylase ... The aldehyde group of this compound is reduced to a primary alcohol using the enzyme glucuronate reductase and the cofactor ... Leferink, N. G.; van den Berg, W. A.; van Berkel, W. J. (2008). "L-Galactono-γ-lactone Dehydrogenase from Arabidopsis thaliana ... L-Galactose reacts with the enzyme L-galactose dehydrogenase, whereby the lactone ring opens and forms again but with between ...
Oxidoreductases: alcohol oxidoreductases (EC 1.1). 1.1.1: NAD/NADP acceptor. *3-hydroxyacyl-CoA dehydrogenase ... Other names in common use include 2-hydroxy-3-carboxyadipate dehydrogenase, 3-carboxy-2-hydroxyadipate dehydrogenase, ... In enzymology, a homoisocitrate dehydrogenase (EC 1.1.1.87) is an enzyme that catalyzes the chemical reaction ... Rowley B, Tucci AF (1970). "Homoisocitric dehydrogenase from yeast". Arch. Biochem. Biophys. 141 (2): 499-, 510. doi:10.1016/ ...
Alcohol is metabolized mainly by the group of six enzymes collectively called alcohol dehydrogenase. These convert the ethanol ... Blood alcohol content (BAC), also called blood alcohol concentration or blood alcohol level, is a measurement of alcohol ... Blood alcohol content, blood ethanol concentration, blood alcohol level, blood alcohol concentration, blood alcohol. ... Furthermore, alcohol dehydrogenase is present in the stomach lining. After absorption, the alcohol passes to the liver through ...
alcohol dehydrogenase (NADP+) activity. • retinal dehydrogenase activity. • allyl-alcohol dehydrogenase activity. • NADP- ... retinol dehydrogenase activity. Cellular component. • mast cell granule. • Schwann cell microvillus. • Schmidt-Lanterman ... dependent enzyme catalyzing the reduction of various aldehydes and ketones to the corresponding alcohol. The involvement in ... dependent enzyme catalyzing the reduction of various aldehydes and ketones to the corresponding alcohol. It also participates ...
catalyzed by retinol dehydrogenases (RDHs)[9] and alcohol dehydrogenases (ADHs).[10] Retinol is called vitamin A alcohol, or ... catalyzed by retinal dehydrogenases[11] also known as retinaldehyde dehydrogenases (RALDHs)[10] as well as retinal oxidases.[12 ... all-trans-retinal + NADPH + H+ → all-trans-retinol + NADP+; all-trans-retinol dehydrogenases, ... 11-cis-retinol + NAD+ → 11-cis-retinal + NADH + H+; 11-cis-retinol dehydrogenases, ...
Positive modulators: Alcohols (e.g., brometone, chlorobutanol (chloretone), ethanol (alcohol), tert-butanol (2M2P), ... Hypotaurine is enzymatically oxidized to yield taurine by hypotaurine dehydrogenase.[2] Hypotaurine (3) is an intermediate in ...
... and consumption of excess alcoholic beverages.[4] Of these, alcohol consumption is the most important.[5] ... and is a possible weak inhibitor of xanthine dehydrogenase. As a byproduct of its fermentation process, beer additionally ... High intake of alcohol (ethanol), a significant cause of hyperuricemia, has a dual action that is compounded by multiple ... Mixed causes include high levels of alcohol and/or fructose in the diet, and starvation. ...
Succinic semialdehyde dehydrogenase deficiency[edit]. Succinic semialdehyde dehydrogenase deficiency is an autosomal-recessive ... List of countries by alcohol consumption per capita *Alcohol consumption by youth in the United States ... The most common example is ethanol (alcohol), which is capable of causing reversible cerebellar and vestibular ataxia. Other ... Non-hereditary causes of cerebellar degeneration include chronic alcohol abuse, head injury, paraneoplastic and non- ...
5-HETE may be further metabolized by 5-Hydroxyeicosanoid dehydrogenase (5-HEDH) to 5-oxo-eicosatetraenoic acid (5-oxo-ETE). ... it may also contribute to hypersensitivity responses of the respiratory system to cold air and possibly even alcohol beverages ... may then be released by the enzyme and rapidly reduced by cellular glutathione peroxidases to its corresponding alcohol, 5(S)- ...
Acute alcohol sensitivity. Alcohol intolerance is due to a genetic polymorphism of the enzyme alcohol dehydrogenase, the enzyme ... Congener (Alcohol congener analysis). *Ethanol (Blood alcohol content, Breathalyzer, Recommended maximum intake of alcoholic ... Alcohol flush reaction. References[edit]. *^ "Acute alcohol sensitivity , Genetic and Rare Diseases Information Center (GARD ... similar to alcohol-containing medications, vinegar, inhalation of alcohol or the vapour of alcohol-containing cleaning agents. ...
retinol dehydrogenase activity. • allyl-alcohol dehydrogenase activity. Cydrannau o'r gell. • cytosol. • extracellular exosome ... alcohol dehydrogenase (NADP+) activity. • protein binding. • aldo-keto reductase (NADP) activity. • L-glucuronate reductase ...
... showed that jet injectors would frequently transmit the viral infection lactate dehydrogenase elevating virus (LDV) from one ... beyond the reach of alcohol swabbing or acetone swabbing)," stated Dr. Bruce Weniger.[15] ...
Drugs: In particular, alcohol, nasal decongestants with adrenergic effects, NSAIDs, MAOIs, adrenoceptor stimulants, and ... Vantyghem MC, Marcelli-Tourvieille S, Defrance F, Wemeau JL (October 2007). "11beta-hydroxysteroide dehydrogenases. Recent ... involves a defect in the gene for 11β-hydroxysteroid dehydrogenase, an enzyme that normally inactivates circulating cortisol to ... by causing inhibition of the 11β-hydroxysteroid dehydrogenase enzyme and likewise leading to secondary apparent ...
Alcohol dehydrogenase. Carbonic anhydrase. DNA polymerase A simple [Fe2S2] cluster containing two iron atoms and two sulfur ...
In bacteria, carbon monoxide is produced via the reduction of carbon dioxide by the enzyme carbon monoxide dehydrogenase, an Fe ...
Livingstone FB (1985). Frequencies of hemoglobin variants: thalassemia, the glucose-6-phosphate dehydrogenase deficiency, G6PD ... Chyka PA, Erdman AR, Christianson G, Wax PM, Booze LL, Manoguerra AS, Caravati EM, Nelson LS, Olson KR, Cobaugh DJ, Scharman EJ ... For example, acetazolamide and ammonium chloride are known to enhance the intoxicating effect of salicylates, and alcohol also ... drink alcohol, take other NSAIDs, or are on other blood thinners.[4] Aspirin is not recommended in the last part of pregnancy.[ ...
After being ingested, the ethanol in alcoholic beverages is first converted to acetaldehyde by the enzyme alcohol dehydrogenase ... This is thought to be caused by declining supplies of alcohol dehydrogenase, the enzyme involved in metabolizing alcohol. ... doi:10.1016/j.alcohol.2007.07.009. PMID 17980785.. *^ Ylikahri R, Heikkonen E, Soukas A (1988). "The sauna and alcohol". Annals ... For example, some people (predominantly East Asians) have a mutation in their alcohol dehydrogenase gene that makes this enzyme ...
... gene silencing of Alcohol dehydrogenase by white-Adh transgenes is Polycomb dependent". Cell. 90 (3): 479-90. doi:10.1016/S0092 ...
"Does alcohol burn off in cooking?". Ochef.com. Hentet 2009-08-29.. ... af acetaldehyd dehydrogenase samt af xanthin oxidase, de to sidstnævnte enzymer hæmmes af et nedbrydningsprodukt af antabus, ... 2003-12-05, Science Daily: Moderate Alcohol Consumption Linked To Brain Shrinkage Citat: "...found a link between low to ... "Our findings do not support the hypothesis that low or moderate alcohol intake offers any protection against cerebral ...
Pal-Bhadra M, Bhadra U, Birchler J (1997). "Cosuppression in Drosophila: gene silencing of Alcohol dehydrogenase by white-Adh ...
Ethanol is dehydrogenated to acetaldehyde by alcohol dehydrogenase, and further into acetic acid by acetaldehyde dehydrogenase ... lactate dehydrogenase A. (subunit M). Human lactate dehydrogenase M4 (the isoenzyme found in skeletal muscle). From PDB: 1I10​. ... D-lactate dehydrogenase, membrane binding. crystal structure of d-lactate dehydrogenase, a peripheral membrane respiratory ... Lactate dehydrogenase-A deficiency is caused by a mutation to the LDHA gene, while lactate dehydrogenase-B deficiency is caused ...
Most of the aldophosphamide is then oxidised by the enzyme aldehyde dehydrogenase (ALDH) to make carboxycyclophosphamide. A ... alcohol, barbiturates, rifampicin, or phenytoin) may result in accelerated metabolism of cyclophosphamide into its active ... Kohn FR, Sladek NE (1985). "Aldehyde dehydrogenase activity as the basis for the relative insensitivity of murine pluripotent ...
Gastrointestinal alcohol dehydrogenase.. Seitz HK1, Oneta CM.. Author information. 1. Department of Medicine, Salem Medical ... Alcohol dehydrogenase (ADH) consists of a family of isozymes that convert alcohols to their corresponding aldehydes using NAD+ ... and its inhibition by alcohol may lead to an alteration of epithelial cell differentiation and cell growth and may also be ... toxic compound that binds to cellular protein and DNA if not further metabolized to acetate by acetaldehyde dehydrogenase ...
Mammalian alcohol dehydrogenase (ADH) constitutes a complex system with different forms and extensive multiplicity (ADH1-ADH6) ... Jörnvall H, Höög J-O. Nomenclature of alcohol dehydrogenases. Alcohol Alcohol 30:153-161;1995.PubMedGoogle Scholar ... Human liver class I alcohol dehydrogenase γγ isozyme: The sole cytosolic 3β-hydroxysteroid dehydrogenase of iso-bile acids. ... Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 Å resolution. J Mol Biol 102:27-59;1976.PubMedGoogle ...
Alcohol dehydrogenase (NAD(P)+) Aldehyde dehydrogenase Oxidoreductase Blood alcohol content for rates of metabolism This ... Edenberg HJ, McClintick JN (October 2018). "Alcohol dehydrogenases, aldehyde dehydrogenases and alcohol use disorders: a ... Edenberg HJ, McClintick JN (December 2018). "Alcohol Dehydrogenases, Aldehyde Dehydrogenases, and Alcohol Use Disorders: A ... alcohol dehydrogenases. Brewers yeast also has another alcohol dehydrogenase, ADH2, which evolved out of a duplicate version ...
Belongs to the zinc-containing alcohol dehydrogenase family. Class-P subfamily.Sequence analysis ... sp,P85440,ADH1_CATRO Alcohol dehydrogenase 1 (Fragments) OS=Catharanthus roseus OX=4058 PE=1 SV=1 ... A secondary alcohol + NAD+ = a ketone + NADH.. ,p>This subsection of the Function section provides information relevant to ... A primary alcohol + NAD+ = an aldehyde + NADH.. ... alcohol dehydrogenase (NAD) activity Source: UniProtKB-EC. * ...
... 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. ...
1994) Purification of acetaldehyde dehydrogenase and alcohol dehydrogenases from Thermoanaerobacter ethanolicus 39E and ... characterization of the secondary-alcohol dehydrogenase (2 degrees Adh) as a bifunctional alcohol dehydrogenase-acetyl-CoA ... Mutant alcohol dehydrogenase leads to improved ethanol tolerance in Clostridium thermocellum. Steven D. Brown, Adam M. Guss, ... Mutant alcohol dehydrogenase leads to improved ethanol tolerance in Clostridium thermocellum. Steven D. Brown, Adam M. Guss, ...
Crystal structure analysis of putative NAD-dependent alcohol dehydrogenase from Thermus thermophilus HB8. Kamiya, N., Hikima, T ...
HADH stands for Horse Liver Alcohol Dehydrogenase. HADH is defined as Horse Liver Alcohol Dehydrogenase rarely. ... The kinetics of the compound of horse liver alcohol dehydrogenase and reduced diphosphopyridine nucleotide. ... www.acronymfinder.com/Horse-Liver-Alcohol-Dehydrogenase-(HADH).html. *Chicago style: Acronym Finder. S.v. "HADH." Retrieved ... www.acronymfinder.com/Horse-Liver-Alcohol-Dehydrogenase-(HADH).html,HADH,/a,. ...
ALCOHOL DEHYDROGENASE E CHAIN(4r)-2-Methylpentane-2,4-DiolNicotinamide-Adenine-Dinucleotide (Acidic Form)TrifluoroethanolZinc ... 4DXH: Horse Liver Alcohol Dehydrogenase Complexed With Nad+ And 2,2,2- Trifluoroethanol. ...
Three anti-horse liver alcohol dehydrogenase (HLADH) monoclonal antibodies are described. Two are specific for ADH and cross- ... Three anti-horse liver alcohol dehydrogenase (HLADH) monoclonal antibodies are described. Two are specific for ADH and cross- ...
Alcohol dehydrogenase 1AAdd BLAST. 375. Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical view ... "Linking of isozyme and class variability patterns in the emergence of novel alcohol dehydrogenase functions. Characterization ... Belongs to the zinc-containing alcohol dehydrogenase family. Class-I subfamily.Curated ... sp,P25405,ADH1A_SAAHA Alcohol dehydrogenase 1A OS=Saara hardwickii OX=40250 PE=1 SV=2 ...
Compare Anti-Alcohol Dehydrogenase 2 Antibody Products from leading suppliers on Biocompare. View specifications, prices, ... Rabbit anti-human zinc binding alcohol dehydrogenase domain containing 2 polyclonal Antibody ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
... specific motifs such as the two zinc-binding domains that bind to the adenosine ribose of the coenzyme and binding to alcohol ... Alcohol dehydrogenase (Adh) is a versatile enzyme involved in many biochemical pathways in plants such as in germination and ... "Characteristics of alcohol/polyol dehydrogenases. The zinc-containing long-chain alcohol dehydrogenases," European Journal of ... Isolation of Alcohol Dehydrogenase cDNA and Basal Regulatory Region from Metroxylon sagu,. International Scholarly Research ...
The retention of the enzyme activity of alcohol dehydrogenase (ADH) has been studied in various drying processes such as spray ... Keywords: alcohol dehydrogenase; encapsulation; spray drying; mannitol alcohol dehydrogenase; encapsulation; spray drying; ... Shiga, H.; Joreau, H.; Neoh, T.L.; Furuta, T.; Yoshii, H. Encapsulation of Alcohol Dehydrogenase in Mannitol by Spray Drying. ... Encapsulation of Alcohol Dehydrogenase in Mannitol by Spray Drying. Hirokazu Shiga 1. ...
Browse our alcohol dehydrogenase 7 Protein catalog backed by our Guarantee+. ... alcohol dehydrogenase 7 Proteins. We offer alcohol dehydrogenase 7 Peptides and alcohol dehydrogenase 7 Proteins for use in ... alcohol dehydrogenase VII protein, alcohol dehydrogenase-7 protein, class IV sigma-1 alcohol dehydrogenase protein, class IV ... Gastric alcohol dehydrogenase protein, Retinol dehydrogenase protein. 3 Results for "alcohol-dehydrogenase-7" in Peptides and ...
Browse our alcohol dehydrogenase 5 Protein catalog backed by our Guarantee+. ... alcohol dehydrogenase 5 Proteins. We offer alcohol dehydrogenase 5 Peptides and alcohol dehydrogenase 5 Proteins for use in ... Alcohol dehydrogenase class chi chain protein, alcohol dehydrogenase class-3 protein, Alcohol dehydrogenase class-III protein, ... Our alcohol dehydrogenase 5 Peptides and alcohol dehydrogenase 5 Proteins can be used in a variety of model species: Human. Use ...
Shop a large selection of products and learn more about Biomatik CorporationHuman Alcohol Dehydrogenase 2 (ADH2) ELISA Kit, 96 ... The Human Alcohol Dehydrogenase 2 (ADH2) ELISA Kit allows for quantitative determination of Alcohol Dehydrogenase 2 in Serum, ... Cross Activity: No significant cross-reactivity or interference between Alcohol Dehydrogenase 2 and analogues was observed. ...
... Östberg, Linus J. Karolinska Inst, Sci Life Lab ... Background: All known attempts to isolate and characterize mammalian class V alcohol dehydrogenase (class V ADH), a member of ... Alcohol dehydrogenase, Mutational pressure, Pseudoenzyme, Sequence analysis, Structural calculations National Category Medical ...
Anti-Alcohol Dehydrogenase antibody (HRP) - Azide free (ab34575) has been cited in 1 publications. Find out more about the ...
What is alcohol dehydrogenase? Meaning of alcohol dehydrogenase medical term. What does alcohol dehydrogenase mean? ... Looking for online definition of alcohol dehydrogenase in the Medical Dictionary? alcohol dehydrogenase explanation free. ... See also: alcohol dehydrogenase (acceptor), alcohol dehydrogenase (NADP+). alcohol dehydrogenase. /al·co·hol de·hy·dro·gen·ase ... alcohol dehydrogenase. Also found in: Dictionary, Acronyms, Encyclopedia, Wikipedia.. Related to alcohol dehydrogenase: ...
HPLC-CD selectivity assay for alcohol dehydrogenases†. Authors. *. Melissa Hamzic,. *Institut für Bioorganische Chemie Heinrich ... This investigation led to an efficient protocol for the alcohol dehydrogenase-catalyzed reduction of 1-phenyl-2-propyn-3- ...
A previously discovered mutant of Saccharomyces cerevisiae alcohol dehydrogenase 1 (Adh1p) was shown to enable a unique NADH- ... Furaldehyde substrate specificity and kinetics of Saccharomyces cerevisiae alcohol dehydrogenase 1 variants. Laadan, B. ...
Alcohol dehydrogenase (ADH) is an enzyme that facilitates the breakdown of alcohols in the body, which could otherwise be toxic ... Computer model showing the structure of human beta3 alcohol dehydrogenase (magenta, blue) with nicotinamide-adenine- ... Caption: Human alcohol dehydrogenase molecule. Computer model showing the structure of human beta3 alcohol dehydrogenase ( ... Alcohol dehydrogenase (ADH) is an enzyme that facilitates the breakdown of alcohols in the body, which could otherwise be toxic ...
Sequence of the gene for a NAD(P)-dependent formaldehyde dehydrogenase (class III alcohol dehydrogenase) from a marine ... Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory ... Formaldehyde dehydrogenase from Pseudomonas putida (PFDH) is a member of the zinc-containing medium-chain alcohol dehydrogenase ... We were unable to measure appreciable levels of NAD(P)-dependent formaldehyde dehydrogenases or alcohol dehydrogenase ...
AcrR and Rex Control Mannitol and Sorbitol Utilization through Their Cross-Regulation of Aldehyde-Alcohol Dehydrogenase (AdhE) ...
Alcohol dehydrogenase class 4 mu/sigma chain. Details. Name. Alcohol dehydrogenase class 4 mu/sigma chain. Kind. protein. ... Alcohol dehydrogenase class 4 mu/sigma chain. P40394. Details. Drug Relations. Drug Relations. DrugBank ID. Name. Drug group. ...
Induction by ethanol of alcohol dehydrogenase activity in Acetobacter pasteurianus.. H Takemura, K Kondo, S Horinouchi, T Beppu ... Induction by ethanol of alcohol dehydrogenase activity in Acetobacter pasteurianus.. H Takemura, K Kondo, S Horinouchi, T Beppu ... Induction by ethanol of alcohol dehydrogenase activity in Acetobacter pasteurianus.. H Takemura, K Kondo, S Horinouchi, T Beppu ... The membrane-bound alcohol dehydrogenase (ADH) activity of Acetobacter pasteurianus NCI1380 was enhanced more than 10-fold by ...
Alcohol dehydrogenase (ADH) is an enzyme that facilitates the break-down of alcohols in the body, which could otherwise be ... Alcohol dehydrogenase, molecular model. Alcohol dehydrogenase (ADH) is an enzyme that facilitates the break-down of alcohols in ... The alcohol is converted to acetaldehyde, an even more toxic molecule, which is then quickly converted into acetate and other ...
Rabbit recombinant monoclonal Alcohol Dehydrogenase antibody [EPR4439] - BSA and Azide free. Validated in WB, IHC, ICC/IF and ... Anti-Alcohol Dehydrogenase antibody [EPR4439] - BSA and Azide free. See all Alcohol Dehydrogenase primary antibodies. ... Primary - Rabbit Anti-Alcohol Dehydrogenase antibody [EPR4439] - BSA and Azide free (ab247607) ICC/IF, WB, IHC-P ... Synthetic peptide within Human Alcohol Dehydrogenase aa 1-100. The exact sequence is proprietary. ...
  • In humans, sequencing of the ADH1B gene (responsible for production of an alcohol dehydrogenase polypeptide) shows several functional variants. (wikipedia.org)
  • Here, we resequence the genome of an ethanol-tolerant mutant, show that the tolerant phenotype is primarily due to a mutated bifunctional acetaldehyde-CoA/alcohol dehydrogenase gene ( adhE ), hypothesize based on structural analysis that cofactor specificity may be affected, and confirm this hypothesis using enzyme assays. (pnas.org)
  • In order to elucidate the mechanism of the ethanol induction, a gene cluster encoding the dehydrogenase and cytochrome c subunits of ADH was cloned from this strain, and its nucleotide sequence was determined. (asm.org)
  • Transcriptional analysis of the cloned genes by primer extension revealed that the gene cluster was transcribed from two different promoters upstream from the dehydrogenase gene. (asm.org)
  • A new study looks at the effects of interplay between peer drinking and the functional variant rs1229984 in the alcohol dehydrogenase 1B gene (ADH1B) among adolescents. (eurekalert.org)
  • A study of the interplay between peer drinking and the functional polymorphism rs1229984 in the alcohol dehydrogenase 1B gene (ADH1B) in the development of adolescent drinking milestones has found that peer drinking reduces the protective effects of an ADH1B variant. (eurekalert.org)
  • For example, some people have a particular variant of the ADH1B gene that causes an amino acid change in this enzyme, which leads to faster enzyme activity so individuals with this variant metabolize alcohol more rapidly which means that acetaldehyde levels are temporarily increased. (eurekalert.org)
  • Molecular and functional characterization of novel glycerol-3-phosphate dehydrogenase 1 like gene (GPD1-L) mutations in sudden infant death syndrome. (harvard.edu)
  • Yasunami M, Chen CS, Yoshida A: A human alcohol dehydrogenase gene (ADH6) encoding an additional class of isozyme. (hmdb.ca)
  • Polymorphism of the human alcohol dehydrogenase 4 (ADH4) promoter affects gene expression. (thefreedictionary.com)
  • Hines' group studied the influence of the gene that encodes alcohol dehydrogenase 3. (thefreedictionary.com)
  • Heterologous expression of the Thermoanaerobacter pseudethanolicus 39E bdhA gene, that encodes an alcohol dehydrogenase, in Clostridium thermocellum significantly increased resistance to furan derivatives at concentrations found in acid-pretreated biomass. (osti.gov)
  • The gene encoding a novel short-chain alcohol dehydrogenase in the thermophilic bacterium, Carboxydothermus hydrogenoformans, was identified and overexpressed in Escherichia coli. (sigmaaldrich.com)
  • This gene encodes class I alcohol dehydrogenase, alpha subunit, which is a member of the alcohol dehydrogenase family. (acris-antibodies.com)
  • The aim of this study is to resolve effects of Si on formation of microstructure and regulation of cinnamyl alcohol dehydrogenase (CAD), a key gene responsible for lignin biosynthesis. (frontiersin.org)
  • Sequence analysis revealed that this gene encodes a pyrrolo-quinoline quinone-dependent alcohol dehydrogenase (ADH). (apsnet.org)
  • Hyun Park, Gene Kidman and Dexter B. Northrop, " Effects of Trehalose on Pressure-Induced Inactivation of Yeast Alcohol Dehydrogenase", Protein & Peptide Letters (2005) 12: 597. (eurekaselect.com)
  • We analyzed effects of single nucleotide polymorphisms (SNP) in the alcohol dehyrdogenase gene cluster (ADH1) and interactions with alcohol consumption in relation to GC risk in a case-control study nested in the EPIC cohort (EurGast). (aacrjournals.org)
  • The gene encoding an alcohol dehydrogenase from T. hypogea was cloned, sequenced and over-expressed. (uwaterloo.ca)
  • Holmes, R. S., 1977, The genetics of a-hydroxyacid oxidase and alcohol dehydrogenase in the mouse: evidence for multiple gene loci and linkage between Hao-2 and Adh-3, Genetics 87:709. (springer.com)
  • Holmes, R. S., 1979a, Genetics and ontogeny of alcohol dehydrogenase isozymes in the mouse - evidence for a cis-acting regulator gene (Adh-3-t) controlling C 2 isozyme expression in reproductive tissues and close linkage of Adh-3 and Adh-3-t on chromosome 3, Biochem. (springer.com)
  • The ABA2 gene product belongs to the family of short-chain dehydrogenases/reductases, which are known to be NAD- or NADP-dependent oxidoreductases. (plantcell.org)
  • Isolation and DNA sequence of ADH3, a nuclear gene encoding the mitochondrial isozyme of alcohol dehydrogenase in Saccharomyces cerevisiae. (asm.org)
  • The Saccharomyces cerevisiae nuclear gene, ADH3, that encodes the mitochondrial alcohol dehydrogenase isozyme ADH III was cloned by virtue of its nucleotide homology to ADH1 and ADH2. (asm.org)
  • A Nonsense Mutation in a Cinnamyl Alcohol Dehydrogenase Gene Is Respon" by Scott E. Sattler, Aaron J. Saathoff et al. (unl.edu)
  • A gene on chromosome 4q23 that encodes a member of the alcohol dehydrogenase family, which metabolise various substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids and lipid peroxidation products. (thefreedictionary.com)
  • The class IV alcohol dehydrogenase gene ADH7 encodes an enzyme that is involved in ethanol and retinol metabolism. (iupui.edu)
  • Yankovsky, N. 2005-12-14 00:00:00 Frequencies of alleles and genotypes for alcohol dehydrogenase gene ADH1B (arg47his polymorphism), associated with alcohol tolerance/sensitivity, were determined. (deepdyve.com)
  • This result gives a third type of evidence, based on purifications and enzyme characterization in lower vertebrates, that the classical liver alcohol dehydrogenase originated by a gene duplication early in the evolution of vertebrates. (diva-portal.org)
  • Murtha, MT & Cavener, DR 1989, ' Ecdysteroid regulation of glucose dehydrogenase and alcohol dehydrogenase gene expression in Drosophila melanogaster ', Developmental biology , vol. 135, no. 1, pp. 66-73. (elsevier.com)
  • A gene encoding a cinnamyl alcohol dehydrogenase homolog in Arabidopsis thaliana. (edu.au)
  • Somers D.A., Nourse J.P., Manners J.M., Abrahams S. and Watson J.M. (1995) A gene encoding a cinnamyl alcohol dehydrogenase homolog in Arabidopsis thaliana. (edu.au)
  • The metabolism of ethanol by gastrointestinal ADH isozymes results in the production of acetaldehyde, a highly toxic compound that binds to cellular protein and DNA if not further metabolized to acetate by acetaldehyde dehydrogenase isozymes. (nih.gov)
  • The metabolism of retinol and the generation of retinoic acid is a function of class I and class IV ADH, and its inhibition by alcohol may lead to an alteration of epithelial cell differentiation and cell growth and may also be involved in ethanol-associated gastrointestinal cocarcinogenesis. (nih.gov)
  • ADH3 (identical to glutathione-dependent formaldehyde dehydrogenase) is clearly the ancestral ADH form and S-hydroxymethylglutathione is the main physiological substrate, but the enzyme can still oxidize ethanol at high concentrations. (springer.com)
  • Cronholm T. Effect of ethanol on the redox state of the coenzyme bound to alcohol dehydrogenase studied in isolated hepatocytes. (springer.com)
  • Induction by ethanol of alcohol dehydrogenase activity in Acetobacter pasteurianus. (asm.org)
  • The membrane-bound alcohol dehydrogenase (ADH) activity of Acetobacter pasteurianus NCI1380 was enhanced more than 10-fold by the addition of ethanol to the medium. (asm.org)
  • Immunoblot analyses showed that almost the same amounts of the cytochrome c and the 15-kDa subunits were produced in both the presence and absence of ethanol and that the amount of the dehydrogenase subunit localized in the membrane was decreased in the absence of ethanol. (asm.org)
  • This incorrect localization of the dehydrogenase subunit might be one of the factors responsible for the low ADH activity in the absence of ethanol. (asm.org)
  • Other names in common use include primary alcohol dehydrogenase, MDH, quinohemoprotein alcohol dehydrogenase, quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase, and alcohol:(acceptor) oxidoreductase. (morebooks.de)
  • Narezode (6-methylpyrazole) is a known competitive inhibitor of alcohol dehydrogenase (12-14) that could substitute for ethanol in the treatment of EG poisoning. (thefreedictionary.com)
  • Today, humans rely on an enzyme called alcohol dehydrogenase 4, or ADH4, to break down ethanol. (thefreedictionary.com)
  • We have developed a recombinant hepatic cell line stably transfected with murine alcohol dehydrogenase cDNA to serve as an in vitro model to investigate these ethanol-induced impairments. (hindawi.com)
  • These results indicate that the ethanol-induced impairment in endocytosis is exacerbated by the inhibition of aldehyde dehydrogenase, suggesting the involvement of acetaldehyde in this dysfunction. (hindawi.com)
  • Class I alcohol dehydrogenase, consisting of several homo- and heterodimers of alpha, beta, and gamma subunits, exhibits high activity for ethanol oxidation and plays a major role in ethanol catabolism. (acris-antibodies.com)
  • Kinetic studies of yeast alcohol dehydrogenase with NAD+ and ethanol, hexanol or decanol as substrates invariably result in non-linear Lineweaver-Burk plots if the alcohol is the variable substrate. (thebiogrid.org)
  • Effects of castration and chronic morphine administration on liver alcohol dehydrogenase and the metabolism of ethanol in the male Sprague-Dawley rat. (aspetjournals.org)
  • The effects of castration on liver alcohol dehydrogenase (ADH) activity and the in vivo metabolism of ethanol were examined in the male Sprague-Dawley-derived rat. (aspetjournals.org)
  • The optimal pHs for ethanol oxidation and acetaldehyde reduction were 10.5 and 7.5 respectively, while the activity for alcohol oxidation was much higher than that of aldehyde reduction. (uwaterloo.ca)
  • The optimal pHs for ethanol oxidation and acetaldehyde reduction were 11.0 and 8.0 respectively, while activity for alcohol oxidation were higher than that of aldehyde reduction. (uwaterloo.ca)
  • This study aims to evaluate the effect of ADH1B and ADH7 genotypes on blood acetaldehyde and ethanol levels after alcohol ingestion, and to measure the genotoxic effect of smoking and ethanol on the buccal cells, also controlling for ADH variants. (separationsnow.com)
  • NADP-dependent isopropanol dehydrogenase belongs to the superfamily of alcohol dehydrogenases with a preference for medium chain secondary alcohols, such as 2- butanol and isopropanol, while it has low activity with primary alcohols, such as ethanol. (creative-enzymes.com)
  • Immunoblot analysis showed that ADH I is detected in cells grown on each alcohol tested, but ethanol was the most effective inducer. (alpfmedical.info)
  • Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 Å resolution. (springer.com)
  • The kinetics of the compound of horse liver alcohol dehydrogenase and reduced diphosphopyridine nucleotide. (acronymfinder.com)
  • Three anti-horse liver alcohol dehydrogenase (HLADH) monoclonal antibodies are described. (springer.com)
  • The role of arginyl residues in directing carboxymethylation of horse liver alcohol dehydrogenase. (harvard.edu)
  • Analysis of rat cytosolic 9-cis-retinol dehydrogenase activity and enzymatic characterization of rat ADHII. (springer.com)
  • Functional characterization of SlscADH1, a fruit-ripening-associated short-chain alcohol dehydrogenase of tomato. (sigmaaldrich.com)
  • Purification and characterization of human liver sorbitol dehydrogenase. (harvard.edu)
  • Biocatalytic characterization of a short-chain alcohol dehydrogenase with broad substrate specificity from thermophilic Carboxydothermus hydrogenoformans. (sigmaaldrich.com)
  • Human liver alcohol dehydrogenase: purification and kinetic characterization of the beta 2 beta 2, beta 2 beta 1, alpha beta 2, and beta 2 gamma 1 "Oriental" isoenzymes. (reactome.org)
  • Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from Saccharomyces cerevisiae. (asm.org)
  • We report here the molecular cloning and characterization of the corresponding cDNA, CAD 1-5, which encodes this novel aromatic alcohol dehydrogenase. (deepdyve.com)
  • The systematic name of this enzyme class is coniferyl-alcohol:NADP+ oxidoreductase. (wikipedia.org)
  • alcohol:NAD+ oxidoreductase, EC 1.1.1.1). (caltech.edu)
  • alcohol:NAD+ oxidoreductase, EC 1.1.1.1) locus in members of the grass family is analyzed. (mysciencework.com)
  • Hoog JO, von Bahr-Lindstrom H, Heden LO, Holmquist B, Larsson K, Hempel J, Vallee BL, Jornvall H: Structure of the class II enzyme of human liver alcohol dehydrogenase: combined cDNA and protein sequence determination of the pi subunit. (hmdb.ca)
  • Ikuta T, Szeto S, Yoshida A: Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence. (hmdb.ca)
  • The expression system was obtained by ligation of a cDNA fragment corresponding to the fl-subunit of human liver alcohol dehydrogenase into the vector pKK 223-3 containing the tac promoter. (portlandpress.com)
  • In the course of engineering these strains, a number of mutations have been discovered in their adhE genes, which encode both alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) enzymes. (asm.org)
  • L2 also possess an alcohol dehydrogenase E (ADHE) that makes them unique among hydrogenosome-bearing anaerobes. (nih.gov)
  • article{d0bd3d3e-39d7-4ff8-8414-d6b625dafbb7, abstract = {Biosensors for measurement of glycerol in FIA were constructed using NAD(+)-dependent glycerol dehydrogenase (GlDH) either co-immobilized with phenazine methosulphate (PMS) or cross-linked to an Os-complex-modified poly(vinylimidazole) redox polymer (PVI(13)dmeOs) using poly(ethyleneglycole) diglycidilether (PEGDGE). (lu.se)
  • Isolation of Π-alcohol dehydrogenase of human liver: Is it a determinant of alcoholism? (springer.com)
  • Marschall H-U, Opperman UCT, Svensson S, Nordling E, Persson B, Höög J-O, Jörnvall H. Human liver class I alcohol dehydrogenase γγ isozyme: The sole cytosolic 3β-hydroxysteroid dehydrogenase of iso-bile acids. (springer.com)
  • The key enzymes involved in alcohol metabolism in the liver are alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). (thefreedictionary.com)
  • Here we report two 1 A resolution crystal structures of liver alcohol dehydrogenase in complex with NADH and two inhibitors: dimethyl sulfoxide and isobutyramide. (lu.se)
  • Human liver alcohol dehydrogenase: purification, composition, and catalytic features. (reactome.org)
  • Ahd-1 (encoding AHD-A 2 ) was found on chromosome 4 near Gpd-1 (encoding the liver isozyme of glucose-6-phosphate dehydrogenase), whereas the aldehyde oxidase loci (Aox-1, Aox-2) were closely linked on chromosome 1 near Id-1 (encoding isocitrate dehydrogenase). (springer.com)
  • The results allow conclusions about the structural and evolutionary relationships within the large family of MDR alcohol dehydrogenases from characterizations of the pigeon (Columba livia) and dogfish (Scyliorhinus canicula) major liver alcohol dehydrogenases. (diva-portal.org)
  • After adjustment for age, daily alcohol consumption and amount of cigarette smoking, significantly increased risks (odds ratios) in the presence of the ALDH2 *2 allele were found for oropharyngolaryngeal (11.14), esophageal (12.50), stomach (3.49), colon (3.35), lung (8.20) and esophageal cancer concomitant with oropharyngolaryngeal and/or stomach cancer (54.20) but not for liver or other cancers. (oup.com)
  • Mammalian alcohol dehydrogenase (ADH) constitutes a complex system with different forms and extensive multiplicity (ADH1-ADH6) that catalyze the oxidation and reduction of a wide variety of alcohols and aldehydes. (springer.com)
  • In analyses of interactions between ADH1 locus SNPs and baseline alcohol consumption, we observed a statistically significant interaction between rs1230025 and beer consumption in relation to GC risk (P value=0.003): variant homozygotes were associated with GC in beer consumers (OR=8.58, 95%CI=3.35-22.0), but not in non-consumers (OR=1.21, 95%CI=0.64-2.30). (aacrjournals.org)
  • Conclusions: Our results suggest that individuals who are heavy consumers of alcohol (specifically beer) and those with certain alleles in the ADH1 locus, and their combination, are at a greater risk for non-cardia gastric adenocarcinoma. (aacrjournals.org)
  • In conclusion, genetic variants at ADH1 and ALDH2 loci may influence GC risk, and alcohol intake may further modify the effect of ADH1 rs1230025. (environment-health.ac.uk)
  • Studies on the properties of the human alcohol dehydrogenase isozymes determined by the different loci ADH1, ADH2, ADH3. (escholarship.org)
  • Alcohol dehydrogenases (ADH) (EC 1.1.1.1) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+) to NADH. (wikipedia.org)
  • The most robust result to emerge from these studies was the demonstration that the genes involved in alcohol metabolism--that is, genes encoding the alcohol dehydrogenase and aldehyde dehydrogenase enzymes--play important roles in the risk for alcoholism (for more information, see the article by Hurley and Edenberg, pp. (thefreedictionary.com)
  • The data presented here can yield a better understanding of alcohol dehydrogenases lacking the catalytic zinc as well as the structural features inherent to thermostable enzymes. (ku.edu)
  • Creative Enzymes is one of the few companies in the world that provides spectrophotometric assays for allyl-alcohol dehydrogenase. (biocatalogue.org)
  • With specialized knowledge in oxidoreductases, especially the ones such as allyl-alcohol dehydrogenase, Creative Enzymes successfully demonstrated the first-in-class test quality and service reliability. (biocatalogue.org)
  • The first step of RA synthesis is controlled by enzymes of the alcohol dehydrogenase (ADH) and retinol dehydrogenase (RDH) families that catalyze oxidation of retinol to retinaldehyde. (ozgene.com)
  • Both of these enzymes contain heme c in addition to PQQ and function as quinohemoprotein dehydrogenases. (alpfmedical.info)
  • Persson B, Zigler JS Jr, Jörnvall H. A superfamily of medium-chain dehydrogenases/reductases (MDR): Sub-lines including ζ-crystallin, alcohol and polyol dehydrogenases, quinone oxidoreductases, enoyl reductases, VAT-1 and other proteins. (springer.com)
  • ADH1A is class I alcohol dehydrogenase, alpha subunit, which is a member of the alcohol dehydrogenase family. (acris-antibodies.com)
  • Altered expression of four proteins, including NADH dehydrogenase flavoprotein 2 (NDUFV2), glyoxalase 1 (GLO1), proteasome subunit beta type 4 (PSMB4, or β7 subunit of proteasome) and nitrilase family, member 2 (Nit2) have been observed between Tg mAPP/DN-RAGE mice cortex and Tg mAPP mice cortex. (bl.uk)
  • We offer alcohol dehydrogenase 7 Peptides and alcohol dehydrogenase 7 Proteins for use in common research applications: ELISA, Protein Array, Western Blot. (novusbio.com)
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  • Background: All known attempts to isolate and characterize mammalian class V alcohol dehydrogenase (class V ADH), a member of the large ADH protein family, at the protein level have failed. (diva-portal.org)
  • The SlscADH1 recombinant protein produced in Escherichia coli exhibited dehydrogenase-reductase activity towards several volatile compounds present in tomato flavour with a strong preference for the NAD/NADH co-factors. (sigmaaldrich.com)
  • Physiological significance of the alcohol dehydrogenase polymorphism in larvae of Drosophila. (thefreedictionary.com)
  • Here we use Drosophila melanogaster alcohol dehydrogenase (ADH) in an experimental test for selective differences between these two mechanisms. (genetics.org)
  • The temporal patterns of glucose dehydrogenase (Gld) and alcohol dehydrogenase (Adh) expression in Drosophila are correlated positively and negatively, respectively, with ecdysterone titers during the late third instar. (elsevier.com)
  • Four additional variants of alcohol and aldehyde dehydrogenases have been purified and functionally characterized, and their primary structures have been determined. (diva-portal.org)
  • Alcohol and aldehyde dehydrogenases: Retinoid metabolic effects in mouse knockout models. (ozgene.com)
  • Those with the variant allele have little tolerance for alcohol, thus lowering chance of dependence and abuse. (wikipedia.org)
  • Alcohol dehydrogenase F allele frequencies Accelerated Control Parental Accelerated p = 1. (thefreedictionary.com)
  • Genetic polymorphism of alcohol dehydrogenase in Europeans: The ADH2*2 allele decreases the risk for alcoholism and is associated with ADH3*1. (thefreedictionary.com)
  • The Human Alcohol Dehydrogenase 2 (ADH2) ELISA Kit allows for quantitative determination of Alcohol Dehydrogenase 2 in Serum, Plasma, Tissue homogenates and other biological fluids. (fishersci.com)
  • The authors examined the association of the alcohol dehydrogenase 2 (ADH2) genotype with vascular events in community-dwelling Japanese (1,102 men/1,093 women). (neurology.org)
  • Enzymatic synthesis of enantiopure aromatic secondary alcohols (including substituted, heteroaromatic and bicyclic structures) were carried out using the halophilic alcohol dehydrogenase ADH2 from Haloferax volcanii (HvADH2). (nottingham.ac.uk)
  • A primary alcohol + NAD + = an aldehyde + NADH. (uniprot.org)
  • A secondary alcohol + NAD + = a ketone + NADH. (uniprot.org)
  • A previously discovered mutant of Saccharomyces cerevisiae alcohol dehydrogenase 1 (Adh1p) was shown to enable a unique NADH-dependent reduction of 5-hydroxymethylfurfural (HMF), a well-known inhibitor of yeast fermentation. (diva-portal.org)
  • In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen. (umassmed.edu)
  • We have determined the X-ray crystal structures of the NADH-dependent alcohol dehydrogenase LlAdhA from Lactococcus lactis and its laboratory-evolved variant LlAdhA^(RE1) at 1.9 Å and 2.5 Å resolution, respectively. (caltech.edu)
  • 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 this study, a novel biocatalyst consisting of magnetic combined cross-linked enzyme aggregates (combi-CLEAs) of 3-quinuclidinone reductase (QNR) and glucose dehydrogenase (GDH) for enantioselective synthesis of ( R )-3-quinuclidinolwith regeneration of cofactors in situ was developed. (mdpi.com)
  • the role of decreased gastric alcohol dehydrogenase and first pass metabolism. (thefreedictionary.com)
  • Metabolism and pharmacokinetics of 3-n-butylphthalide (NBP) in humans: the role of cytochrome P450s and alcohol dehydrogenase in biotransformation. (curehunter.com)
  • Aldehyde dehydrogenase-2 (ALDH2) eliminates most of the acetaldehyde produced during alcohol metabolism. (oup.com)
  • Alcohol dehydrogenase (ADH) consists of a family of isozymes that convert alcohols to their corresponding aldehydes using NAD+ as a cofactor. (nih.gov)
  • In humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in generation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. (wikipedia.org)
  • The alcohol dehydrogenases comprise a group of several isozymes that catalyse the oxidation of primary and secondary alcohols to aldehydes and ketones, respectively, and also can catalyse the reverse reaction. (wikipedia.org)
  • Alcohol dehydrogenase (ADH) is an enzyme that facilitates the breakdown of alcohols in the body, which could otherwise be toxic. (sciencephoto.com)
  • ADH functions primarily in the detoxification of ingested alcohols, and it is thought that the evolution of this enzyme, accompanied by adaptation to survival in alcohol-rich environments such as rotting fruits, has played an important role in the evolution of the family Drosophilidae, particularly the subfamily Drosophilinae ( A shburner 1998 ). (genetics.org)
  • Cinnamyl alcohol dehydrogenase is a zinc- and NADPH-dependent dehydrogenase catalyzing the reversible conversion of p-hydroxycinnamaldehydes to their corresponding hydroxycinnamyl alcohols. (unboundmedicine.com)
  • Kinetics and reaction mechanism of yeast alcohol dehydrogenase with long-chain primary alcohols. (thebiogrid.org)
  • The kinetic coefficients determined from secondary plots are consistent with an 'equilibrium random-order' mechanism for extremely low alcohol concentrations and for all alcohols, the transformation of the ternary complexes being the rate-limiting step of the reaction. (thebiogrid.org)
  • Alcohol dehydrogenase (ADH) is a key enzyme responsible for alcohol production, catalyzing interconversions between alcohols and corresponding ketones or aldehydes. (uwaterloo.ca)
  • Rising Demand to Produce Pure Stereoisomers of Chiral Alcohols is also expected to contribute significantly to the Alcohol Dehydrogenase market. (advancemarketanalytics.com)
  • Alcohol substrates: Seventeen different alcohols were tested. (escholarship.org)
  • Only a limited number of studies have investigated the interplay between specific robust genes associated with the development of alcohol dependence and environments during the critical developmental period of adolescence," said Bierut. (eurekalert.org)
  • Disruption of the genes encoding both cinnamyl alcohol dehydrogenases ( CADs ), including CADC and CADD , in Arabidopsis thaliana results in the atypical incorporation of hydroxycinnamaldehydes into lignin. (plantcell.org)
  • In contrast with the report the alcohol dehydrogenase activity in gastric mucosa is lower in women than in men[6], in this small study we noted no significant difference in activities between the sexes. (thefreedictionary.com)
  • Genetic variation in alcohol dehydrogenase (ADH1A, ADH1B, ADH1C, ADH7) and aldehyde dehydrogenase (ALDH2), alcohol consumption and gastric cancer risk in the European Prospective Investigation into Cancer and Nutrition (EPIC) cohort. (environment-health.ac.uk)
  • Studies that have examined the association between alcohol consumption and gastric cancer (GC) risk have been inconsistent. (environment-health.ac.uk)
  • The first-ever isolated alcohol dehydrogenase (ADH) was purified in 1937 from Saccharomyces cerevisiae (brewer's yeast). (wikipedia.org)
  • An NADP-dependent branched-chain alcohol dehydrogenase was purified from Saccharomyces cerevisiae var. (asm.org)
  • In enzymology, a coniferyl-alcohol dehydrogenase (EC 1.1.1.194) is an enzyme that catalyzes the chemical reaction coniferyl alcohol + NADP+ ⇌ {\displaystyle \rightleftharpoons } coniferyl aldehyde + NADPH + H+ Thus, the two substrates of this enzyme are coniferyl alcohol and NADP+, whereas its 3 products are coniferyl aldehyde, NADPH, and H+. (wikipedia.org)
  • Along with this, the Global Alcohol Dehydrogenase market size has been validated using both top-down and bottom-up approaches. (advancemarketanalytics.com)
  • The Global Alcohol Dehydrogenase market size will be XX million (USD) in 2023, from the XX million (USD) in 2017, with a CAGR (Compound Annual Growth Rate) of XX% from between 2017 and 2023. (reportsnreports.com)
  • The structure of HpCAD is highly homologous to the sinapyl alcohol dehydrogenase and the plant CAD with well-conserved residues involved in catalysis and zinc binding. (unboundmedicine.com)
  • Enzyme activity and substrate specificity of the major cinnamyl alcohol dehydrogenases in sorghum. (plantphysiol.org)
  • 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)
  • Isozymes of yeast alcohol dehydrogenase are slowly denatured at moderate hydrostatic pressures ( (eurekaselect.com)
  • Alcohol dehydrogenase derived from yeast is a metalloenzyme containing four tightly bound zinc atoms per molecule (Vallee and Hoch, Proc. (p212121.com)
  • The retention of the enzyme activity of alcohol dehydrogenase (ADH) has been studied in various drying processes such as spray drying. (mdpi.com)
  • Cross Activity: No significant cross-reactivity or interference between Alcohol Dehydrogenase 2 and analogues was observed. (fishersci.com)
  • A CAD homolog from Helicobacter pylori (HpCAD) possesses broad substrate specificities like the plant CADs and additionally a dismutation activity converting benzaldehyde to benzyl alcohol and benzoic acid. (unboundmedicine.com)
  • Combining detailed structural information and directed evolution, we have achieved significant improvements in non-native alcohol dehydrogenase activity that will facilitate the production of next-generation fuels such as isobutanol from renewable resources. (caltech.edu)
  • Can genetics predict risk for alcohol dependence? (thefreedictionary.com)
  • Holmes, R.S., 1978b, Genetics and ontogeny of aldehyde dehydrogenase isozymes in the mouse: localization of Ahd-1 encoding the mitochondrial isozymes on chromosome 4, Biochem. (springer.com)
  • Expression of alcohol dehydrogenase 3 (ADH3) in tissue and cultured cells from human oral mucosa. (springer.com)
  • Given the toxicity of acetaldehyde, negative effects are experienced by people with this ADH1B variant when they drink alcohol, which discourages heavy drinking and serves as a protective effect. (eurekalert.org)
  • Because peer drinking is known to have a strong effect on youth alcohol use, we hypothesized that this important environmental influence would alter the effect of the ADH1B variant on early drinking milestones, such as becoming intoxicated or experiencing a symptom of an AUD. (eurekalert.org)
  • Study authors selected 1,550 European and African-American individuals (766 females, 784 males) who had a full drink of alcohol before age 18, since the ADH1B variant is expected to exhibit a protective effect only in response to alcohol consumption. (eurekalert.org)
  • A known functional SNP in ADH1B (rs1229984) was associated with alcohol intake (P-value = 0.04) but not GC risk. (environment-health.ac.uk)
  • The putative basal msAdh 1 regulatory region was further determined to contain promoter signals of TATA and AGGA boxes and predicted amino acids analyses showed several Adh -specific motifs such as the two zinc-binding domains that bind to the adenosine ribose of the coenzyme and binding to alcohol substrate. (hindawi.com)
  • Belongs to the zinc-containing alcohol dehydrogenase family. (abcam.com)
  • It is highly specific for benzyl alcohol. (mybiosource.com)
  • Also known as Aryl-alcohol dehydrogenase (Benzyl alcohol dehydrogenase) (BADH). (mybiosource.com)
  • Our alcohol dehydrogenase 7 Peptides and alcohol dehydrogenase 7 Proteins can be used in a variety of model species: Human. (novusbio.com)
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  • Comparison of the deduced amino acid sequences and the NH2-terminal sequences determined with purified proteins showed that the dehydrogenase and cytochrome c subunits contained typical signal peptides of 35 and 26 amino acids, respectively. (asm.org)
  • Also known as Aryl-alcohol dehydrogenase [NADP(+)] (AAD). (mybiosource.com)
  • In enzymology, an alcohol dehydrogenase (acceptor) (EC 1.1.99.8) is an enzyme that catalyzes the chemical reaction a primary alcohol + acceptor \rightleftharpoons an aldehyde + reduced acceptor Thus, the two substrates of this enzyme are primary alcohol and acceptor, whereas its two products are aldehyde and reduced acceptor. (morebooks.de)
  • Niederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD: Three-dimensional structures of the three human class I alcohol dehydrogenases. (hmdb.ca)
  • Human alcohol dehydrogenase molecule. (sciencephoto.com)
  • Computer model showing the structure of human beta3 alcohol dehydrogenase (magenta, blue) with nicotinamide-adenine-dinucleotides shown in green. (sciencephoto.com)
  • Synthetic peptide within Human Alcohol Dehydrogenase aa 1-100. (abcam.com)
  • Human alcohol dehydrogenase (ADH, tiff isozyme of class I) was expressed in Escherichia coli, purified to homogeneity, and characterized regarding N-terminal processing. (portlandpress.com)
  • Using M3-2 and 11-hydroxy-NBP as substrates, human subcellular fractions experiments revealed that P450, alcohol dehydrogenase , and aldehyde dehydrogenase catalyzed the generation of M2 and M5-2. (curehunter.com)