Alcohol Dehydrogenase: 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.Alcohol Oxidoreductases: 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).Alcohol Drinking: Behaviors associated with the ingesting of alcoholic beverages, including social drinking.Alcohols: 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)Ethanol: 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.L-Lactate Dehydrogenase: 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.Aldehyde Dehydrogenase: 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.NAD: 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)Aldehyde Oxidoreductases: Oxidoreductases that are specific for ALDEHYDES.L-Iditol 2-Dehydrogenase: 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 1.1.1.14Acetaldehyde: 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.Horses: 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.Glyceraldehyde-3-Phosphate Dehydrogenases: 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.Sugar Alcohol Dehydrogenases: 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.Malate Dehydrogenase: An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.Glutamate Dehydrogenase: 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.Glucosephosphate DehydrogenaseKinetics: The rate dynamics in chemical or physical systems.Isocitrate Dehydrogenase: 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.Benzyl Alcohols: Alcohols derived from the aryl radical (C6H5CH2-) and defined by C6H5CHOH. The concept includes derivatives with any substituents on the benzene ring.Butanols: Isomeric forms and derivatives of butanol (C4H9OH).Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Molecular Sequence Data: 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.Alcoholism: 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)Carbohydrate Dehydrogenases: 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.Amino Acid Sequence: 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.Isoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.Benzyl Alcohol: 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.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Glucose 1-Dehydrogenase: A glucose dehydrogenase that catalyzes the oxidation of beta-D-glucose to form D-glucono-1,5-lactone, using NAD as well as NADP as a coenzyme.Glycerolphosphate DehydrogenaseDihydrolipoamide Dehydrogenase: 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.Succinate Dehydrogenase: 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.NADP: 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)Coenzymes: Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.Oxidation-Reduction: 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).1-Propanol: A colorless liquid made by oxidation of aliphatic hydrocarbons that is used as a solvent and chemical intermediate.Hydroxysteroid Dehydrogenases: Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.BenzaldehydesAldehydes: Organic compounds containing a carbonyl group in the form -CHO.Glucose Dehydrogenases: 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.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Oxidoreductases: 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)Cloning, Molecular: 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.Ketoglutarate Dehydrogenase ComplexMannitol Dehydrogenases: Sugar alcohol dehydrogenases that have specificity for MANNITOL. Enzymes in this category are generally classified according to their preference for a specific reducing cofactor.3-Hydroxyacyl CoA Dehydrogenases: 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.17-Hydroxysteroid Dehydrogenases: A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.Methanol: 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.3-Hydroxysteroid Dehydrogenases: Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.Phosphogluconate Dehydrogenase: 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.Acetobacter: 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.NADH Dehydrogenase: 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.Acyl-CoA Dehydrogenases: Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.Propanols: Isomeric forms and derivatives of PROPANOL (C3H7OH).IMP Dehydrogenase: An enzyme that catalyzes the dehydrogenation of inosine 5'-phosphate to xanthosine 5'-phosphate in the presence of NAD. EC 1.1.1.205.Hydroxybutyrate DehydrogenaseHydrogen-Ion Concentration: 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)Lactate Dehydrogenases: Alcohol oxidoreductases with substrate specificity for LACTIC ACID.PQQ Cofactor: 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.Alcoholic Intoxication: An acute brain syndrome which results from the excessive ingestion of ETHANOL or ALCOHOLIC BEVERAGES.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Formate Dehydrogenases: 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.Central Nervous System Depressants: 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).Acyl-CoA Dehydrogenase: 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.Xanthine Dehydrogenase: 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.Zinc: 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.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Pyruvate Decarboxylase: 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.Gram-Positive Asporogenous Rods, Irregular: A group of irregular rod-shaped bacteria that stain gram-positive and do not produce endospores.3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide): 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.Retinal Dehydrogenase: 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.Fermentation: 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.Fetal Alcohol Spectrum Disorders: 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.Escherichia coli: 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.Alcoholic Beverages: Drinkable liquids containing ETHANOL.Pyruvate Dehydrogenase (Lipoamide): 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).PropaneKetone Oxidoreductases: Oxidoreductases that are specific for KETONES.11-beta-Hydroxysteroid Dehydrogenases: 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, Starch Gel: Electrophoresis in which a starch gel (a mixture of amylose and amylopectin) is used as the diffusion medium.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Lignin: 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)Uridine Diphosphate Glucose Dehydrogenase: An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.Dihydrouracil Dehydrogenase (NADP): An oxidoreductase involved in pyrimidine base degradation. It catalyzes the catabolism of THYMINE; URACIL and the chemotherapeutic drug, 5-FLUOROURACIL.Pentanols: Isomeric forms and derivatives of pentanol (C5H11OH).Gluconobacter: 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)Protein Conformation: 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).Stereoisomerism: 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)Pseudomonas: A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.Gene Expression Regulation, Enzymologic: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.Molecular Weight: The sum of the weight of all the atoms in a molecule.Drosophila melanogaster: A species of fruit fly much used in genetics because of the large size of its chromosomes.Glucosephosphate Dehydrogenase Deficiency: 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.Saccharomyces cerevisiae: 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.Enzyme Stability: 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.Alanine Dehydrogenase: 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.Mutation: 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.11-beta-Hydroxysteroid Dehydrogenase Type 1: 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.Zymomonas: 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.3-alpha-Hydroxysteroid Dehydrogenase (B-Specific): 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.Disulfiram: 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, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Butylene Glycols: 4-carbon straight chain aliphatic hydrocarbons substituted with two hydroxyl groups. The hydroxyl groups cannot be on the same carbon atom.Fatty Alcohols: 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)Species Specificity: 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.Hexanols: Isomeric forms and derivatives of hexanol (C6H11OH).Hydroxyprostaglandin Dehydrogenases: Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.Hydroxysteroids: 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.Octanols: Isomeric forms and derivatives of octanol (C8H17OH).Alcohol-Related Disorders: Disorders related to or resulting from abuse or mis-use of alcohol.Spectrophotometry: The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+)Butyryl-CoA Dehydrogenase: 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.Acinetobacter calcoaceticus: 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.KetonesGenes: 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.Genes, Bacterial: The functional hereditary units of BACTERIA.Alcohol Deterrents: 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.Anaerobiosis: 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)20-Hydroxysteroid Dehydrogenases: 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).2-Propanol: 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.Acetone: A colorless liquid used as a solvent and an antiseptic. It is one of the ketone bodies produced during ketoacidosis.Multienzyme Complexes: 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, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Acinetobacter: A genus of gram-negative bacteria of the family MORAXELLACEAE, found in soil and water and of uncertain pathogenicity.Chemistry: A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.11-beta-Hydroxysteroid Dehydrogenase Type 2: 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.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Sequence Alignment: 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.Chemical Phenomena: The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.Polyvinyl Alcohol: 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, Immobilized: 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.Acyl-CoA Dehydrogenase, Long-Chain: 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.Formates: 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.Homoserine Dehydrogenase: 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.Iodoacetates: Iodinated derivatives of acetic acid. Iodoacetates are commonly used as alkylating sulfhydryl reagents and enzyme inhibitors in biochemical research.Benzaldehyde Dehydrogenase (NADP+)Temperature: 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.Pseudomonas putida: A species of gram-negative, aerobic bacteria isolated from soil and water as well as clinical specimens. Occasionally it is an opportunistic pathogen.Isovaleryl-CoA Dehydrogenase: 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).3-Isopropylmalate Dehydrogenase: 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.Mandelic Acids: Analogs or derivatives of mandelic acid (alpha-hydroxybenzeneacetic acid).Pyrazoles: 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.Cortisone Reductase: 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.Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.Malate Dehydrogenase (NADP+)tert-Butyl AlcoholPyruvate Dehydrogenase (Lipoamide)-Phosphatase: (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.Leucine Dehydrogenase: 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+.Phosphoglycerate Dehydrogenase: An enzyme that catalyzes the oxidation of 3-phosphoglycerate to 3-phosphohydroxypyruvate. It takes part in the L-SERINE biosynthesis pathway.RNA, Messenger: 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.Protein Binding: 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.Restriction Mapping: Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.Propylene Glycol: A clear, colorless, viscous organic solvent and diluent used in pharmaceutical preparations.Spectrophotometry, Ultraviolet: 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)PyruvatesEstradiol Dehydrogenases: 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 1.1.1.62Sequence Homology, Nucleic Acid: The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.Benzyl CompoundsPlasmids: 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.D-Xylulose Reductase: 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+.Bacterial Proteins: Proteins found in any species of bacterium.Spectrometry, Fluorescence: Measurement of the intensity and quality of fluorescence.Glutamate Dehydrogenase (NADP+)Thermoanaerobacter: A genus of gram-positive, anaerobic bacteria in the family Thermoanaerobacteriaceae. Cultures consist of rods interspersed with coccoid cells.Succinate-Semialdehyde Dehydrogenase: 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).Hydrogen: 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.Macromolecular Substances: 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.PhenanthrolinesButanesMitochondria: Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)Formic Acid EstersEnzyme Induction: 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, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.Glucose: 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.Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating): 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.Multigene Family: 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)Acetates: Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.Models, Chemical: Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.Vitamin A: 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.Pseudomonadaceae: A family of gram-negative bacteria usually found in soil or water and including many plant pathogens and a few animal pathogens.Acetoin: A product of fermentation. It is a component of the butanediol cycle in microorganisms. In mammals it is oxidized to carbon dioxide.1-Butanol: A four carbon linear hydrocarbon that has a hydroxy group at position 1.Lactobacillus brevis: 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.Xylitol: 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.Clostridium: 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.Cobalt: 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.Cyclohexanols: 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.Hot Temperature: Presence of warmth or heat or a temperature notably higher than an accustomed norm.Oxidoreductases Acting on CH-CH Group Donors: 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.Apoenzymes: 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.Toluene: A widely used industrial solvent.Alcohol-Induced Disorders: Disorders stemming from the misuse and abuse of alcohol.Prephenate Dehydrogenase: 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.Genotype: The genetic constitution of the individual, comprising the ALLELES present at each GENETIC LOCUS.Genetic Variation: Genotypic differences observed among individuals in a population.AcroleinMethylphenazonium Methosulfate: 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.Geobacillus stearothermophilus: 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.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.

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)

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, ...
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.[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, ...
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, ...
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 ...
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 ...
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 ...
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 ...
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
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
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.
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.
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 ...
Zinc in PDB 3fsr: Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of T. Brockii Adh By C. Beijerinckii Adh
Alcohol consumption is a risk factor for the development of certain types of cancer. However, understanding why that might be has remained elusive. Now, Silvia Balbo suggests that a new study could have implications for hundreds of millions of drinkers of Asian descent. Balbo works with cancer prevention expert Stephen Hecht at the University of Minnesota. Speaking at the 244thNational Meeting & Exposition of the American Chemical Society in Philadelphia, she explained how acetaldehyde formed by natural metabolism of the ethanol from alcoholic beverages causes damage to DNA. "Acetaldehyde attaches to DNA in humans - to the genetic material that makes up genes - in a way that results in the formation of a DNA adduct. Its acetaldehyde that latches onto DNA and interferes with DNA activity in a way linked to an increased risk of cancer," she said. One in three people of Asian descent, which includes Native Americans and Native Alaskans have a variant on the enzyme alcohol dehydrogenase, which ...
Alcohol dehydrogenase derived from yeast is a metalloenzyme containing four tightly bound zinc atoms per molecule (Vallee and Hoch, Proc. Natl. Acad. Sci. USA, 41, 327, 1955). The optimum pH for the enzymatic oxidation of ethanol is 8.6-9.0 and is closer to 7.0 for the reduction of acetaldehyde.. ...
Endogenous S-nitrosothiols, including S-nitrosoglutathione (GSNO), mediate nitric oxide (Zero)-structured signaling, inflammatory responses, and simple muscle function. for individual GSNOR with reduced combination reactivity to various other ADH protein. We verified the current presence of GSNOR in 85% of specimens analyzed, and extensive evaluation of these examples confirmed no difference in GSNOR proteins appearance between cancerous and regular lung tissue. Additionally, GSNOR and various other ADH mRNA amounts were examined quantitatively in lung cancers cDNA arrays by qPCR. In keeping with our immunohistochemical results, GSNOR mRNA amounts were not transformed in lung cancers tissues, nevertheless the expression degrees of various other ADH genes had been reduced. ADH IB mRNA amounts were decreased ( 10-flip) in 65% from the lung cancers cDNA specimens. We conclude the fact that previously LY 255283 reported outcomes showed an wrong association of GSNOR and individual lung cancers risk, ...
According to our results, a normal E. coli cell extract has a dodecanol-1 dehydrogenase activity of 9.64e-12 kat/mg (0.58 mU/mg); whereas our recombinant strain 018A has an activity of 2.93e-11 kat/mg (1.76 mU/mg). According to our analysis, the enzymatic activities of both strains are statistically different at confidence level of 0.95, which means that the part BBa_K398018 increases 2 times the alcohol dehydrogenase activity in the cell extract. We can conclude from our data that the parts BBa_K398005 and BBa_K398018 have biological activity; particularly when we used BBa_K398018 the enzyme activity of E. coli cell extracts became equivalent to 3% of the in vitro activity of the positive control (Pseudomonas putida). A comparison of both activities maybe it is not interesting from the functional point of view, since those differences could be related to substrate affinity or discrepancies in the optimal pH. However, we think that from this comparison of both in vitro activities we can suggest ...
According to our results, a normal E. coli cell extract has a dodecanol-1 dehydrogenase activity of 9.64e-12 kat/mg (0.58 mU/mg); whereas our recombinant strain 018A has an activity of 2.93e-11 kat/mg (1.76 mU/mg). According to our analysis, the enzymatic activities of both strains are statistically different at confidence level of 0.95, which means that the part BBa_K398018 increases 2 times the alcohol dehydrogenase activity in the cell extract. We can conclude from our data that the parts BBa_K398005 and BBa_K398018 have biological activity; particularly when we used BBa_K398018 the enzyme activity of E. coli cell extracts became equivalent to 3% of the in vitro activity of the positive control (Pseudomonas putida). A comparison of both activities maybe it is not interesting from the functional point of view, since those differences could be related to substrate affinity or discrepancies in the optimal pH. However, we think that from this comparison of both in vitro activities we can suggest ...
ADH4, class II alcohol dehydrogenase 4 pi subunit, which is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a…
Adr1 and Cat8 play different roles at ADH2 and FBP1.Comparison between the ADH2 (A and C, orange) and FBP1 (B and D, blue) promoters in either adr1Δ (A and B)
Kit Component:- KN209616G1, ADH1C gRNA vector 1 in pCas-Guide vector- KN209616G2, ADH1C gRNA vector 2 in pCas-Guide vector- KN209616D, donor vector…
Dear Kausik,. Thank you for reading and commenting on our recent study. Yes, the difficulties in detecting the ethanol were frustrating for us as it prevented us from definitively attributing the in vivo phenotype of the alcC mutant to loss of ethanol production. The lack of cell wall alteration in the mutant argues strongly for a secreted factor being responsible, but without the robust ethanol data, we could not definitively state the mechanism to be due to ethanol. We are working on detecting EtOH in live animals, so it can be monitored over the time course of infection to further improve our understanding of the fungal-host interaction.. With regard to the immunosuppression, the effects of triamcinolone and cyclophosphamide on the immune system are complex and still not fully understood. One important point: while the doses of cyclophosphamide used in our model and other murine models of IPA do induce leukopenia, most often this has been measured in uninfected animals. For example, see the ...
Catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs (By similarity).
NADP-dependent oxidoreductase, putative; FUNCTIONS IN: oxidoreductase activity, binding, catalytic activity, zinc ion binding; INVOLVED IN: response to oxidative stress, response to cyclopentenone; EXPRESSED IN: 11 plant structures; EXPRESSED DURING: LP.06 six leaves visible, 4 anthesis, LP.04 four leaves visible, petal differentiation and expansion stage; CONTAINS InterPro DOMAIN/s: GroES-like (InterPro:IPR011032), NAD(P)-binding (InterPro:IPR016040), Alcohol dehydrogenase, zinc-binding (InterPro:IPR013149), Alcohol dehydrogenase superfamily, zinc-containing (InterPro:IPR002085); BEST Arabidopsis thaliana protein match is: AT-AER (alkenal reductase); 2-alkenal reductase (TAIR:AT5G16970.1); Has 10893 Blast hits to 10880 proteins in 1040 species: Archae - 76; Bacteria - 5027; Metazoa - 696; Fungi - 750; Plants - 299; Viruses - 0; Other Eukaryotes - 4045 (source: NCBI BLink ...
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... 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 ... NAD+ This reaction is catalyzed by alcohol dehydrogenase (ADH1 in baker's yeast). As shown by the reaction equation, glycolysis ... phenylethyl alcohol and gamma-butyrolactone, secondary products of alcoholic fermentation". Comptes rendus hebdomadaires des ... The overall chemical formula for alcoholic fermentation is: C 6 H 12 O 6 ⟶ 2 C 2 H 5 OH + 2 CO 2 {\displaystyle {\ce {C6H12O6 ...
Thomson JM, Gaucher EA, Burgan MF, De Kee DW, Li T, Aris JP, Benner SA (2005). "Resurrecting ancestral alcohol dehydrogenases ... The occurrence of alcoholic fermentation is not primarily due to a limited respiratory capacity. ... alcohol) in aerobic conditions and high external glucose concentrations rather than producing biomass via the tricarboxylic ...
... a putative alcohol dehydrogenase gene (btrE, neo5); another putative dehydrogenase (similar to chorine dehydrogenase and ...
This gene encodes class I alcohol dehydrogenase, gamma subunit, which is a member of the alcohol dehydrogenase family. Members ... Class I alcohol dehydrogenase, consisting of several homo- and heterodimers of alpha, beta, and gamma subunits, exhibits high ... "Entrez Gene: ADH1C alcohol dehydrogenase 1C (class I), gamma polypeptide". Human ADH1C genome location and ADH1C gene details ... Xu YL, Carr LG, Bosron WF, Li TK, Edenberg HJ (Apr 1988). "Genotyping of human alcohol dehydrogenases at the ADH2 and ADH3 loci ...
Gupta, N. K.; Woodley, C. L.; Fried, R. (1970). "Effect of metronidazole on liver alcohol dehydrogenase". Biochemical ... Consuming alcohol while taking metronidazole has long been thought to have a disulfiram-like reaction with effects that can ... Consumption of alcohol is typically advised against by patients during systemic metronidazole therapy and for at least 48 hours ... However, some studies call into question the mechanism of the interaction of alcohol and metronidazole, and a possible central ...
It competitively inhibits alcohol dehydrogenase for example. Oxidation of trifluoroethanol yields trifluoroacetaldehyde or ... Also known as TFE or trifluoroethyl alcohol, this colourless, water-miscible liquid has a smell reminiscent of ethanol. Due to ... the electronegativity of the trifluoromethyl group, this alcohol exhibits a stronger acidic character compared to ethanol. Thus ...
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 ...
Crystallization of Sulfolobus Solfataricus Alcohol Dehydrogenase experiment; Crystallization of Turnip Yellow Mosaic Virus, ...
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". Human ADH4 genome location and ADH4 gene ...
Salisbury SA, Forrest HS, Cruse WB, Kennard O (1979). "A novel coenzyme from bacterial primary alcohol dehydrogenases". Nature ... Anthony and Zatman also found the unknown redox cofactor in alcohol dehydrogenase. In 1979, Salisbury and colleagues as well as ... Glucose dehydrogenase, one of the quinoproteins, is used as a glucose sensor. PQQ stimulates growth in bacteria. It was ... Hauge JG (1964). "Glucose dehydrogenase of bacterium anitratum: an enzyme with a novel prosthetic group". J Biol Chem. 239: ...
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, G. R.; Carr, N. G. (1970). "A novel alcohol dehydrogenase present in Rhodomicrobium vannielii". Archiv für ...
Salisbury SA, Forrest HS, Cruse WB, Kennard O (August 1979). "A novel coenzyme from bacterial primary alcohol dehydrogenases". ... An example of this are the dehydrogenases that use nicotinamide adenine dinucleotide (NAD+) as a cofactor. Here, hundreds of ... For example, the multienzyme complex pyruvate dehydrogenase at the junction of glycolysis and the citric acid cycle requires ... PMC 2786976 . PMID 19693930 Harden A, Young WJ (24 October 1906). "The Alcoholic Ferment of Yeast-Juice". Proceedings of the ...
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 ...
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". J ... 1999). "17Beta-hydroxysteroid dehydrogenases in human bone cells". J. Bone Miner. Res. 13 (10): 1539-46. doi:10.1359/jbmr. ... 1999). "17Beta-hydroxysteroid dehydrogenase type 1, 2, 3, and 4 expression and enzyme activity in human anterior pituitary ...
These ions can inhibit oxidative enzymes such as yeast alcohol dehydrogenase. Silver ions have also been shown to interact with ... "Effects of silver and mercurials on yeast alcohol dehydrogenase". J. Biol. Chem. 235: 504-508. Russell, A. D.; Hugo, W. B. ( ...
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 ... Ethylene glycol is first metabolized to glycolaldehyde by the enzyme alcohol dehydrogenase, which then undergoes further ... Methanol is first metabolized to formaldehyde by alcohol dehydrogenase. It then undergoes subsequent oxidation via formaldehyde ...
... 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 ...
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- ...
12(9): p. 3983-4000 Dennis, E.S., et al., Molecular analysis of the alcohol dehydrogenase 2 (Adh2) gene of maize. Nucleic Acids ... Dennis, E.S., et al., Molecular analysis of the alcohol dehydrogenase (Adh1) gene of maize. Nucleic Acids Research, 1984. ... She, together with her collaborators, cloned the gene encoding the enzyme alcohol dehydrogenase and identified the regulatory ...
This latter compound is transformed to tryptophol by alcohol dehydrogenase. It is formed from tryptophan, along with indole-3- ... phenylethyl alcohol and gamma-butyrolactone, secondary products of alcoholic fermentation". Comptes Rendus de l'Académie des ... It is also found in wine as a secondary product of alcoholic fermentation. It was first described by Felix Ehrlich in 1912. ... Tryptophol is an aromatic alcohol that induces sleep in humans. It is formed in the liver after disulfiram treatment. It is ...
Pervasive and required for several enzymes such as carboxypeptidase, liver alcohol dehydrogenase, and carbonic anhydrase ...
Degrades cellulose Produces alcohol dehydrogenase Produces ethyl alcohol ethanol Production of ethanol from cellulose ... Purification and properties of primary and secondary alcohol dehydrogenases from Thermoanaerobacter ethanolicus. Appl. Environ ...
Fetal alcohol spectrum disorder (FASD) is a term that is used to describe the range of effects that can occur in an individual ... Prenatal exposure to alcohol is a leading preventable cause of birth defects and developmental disabilities. ... Protective effects of the alcohol dehydrogenase-ADH1B allele in children exposed to alcohol during pregnancy. J Pediatr 2006; ... Alcohol Alcohol 2016; 51:367.. *Bertrand J, Floyd RL, Weber MK, et al. National Task Force on Fetal alcohol syndrome and fetal ...
... alcohol). Disulfiram works by inhibiting the enzyme acetaldehyde dehydrogenase, which means many of the effects of a "hangover ... Disulfiram blocks the oxidation of alcohol at the acetaldehyde stage. Disulfiram is also being studied as a treatment for ... Disulfiram produces a sensitivity to alcohol which results in a highly unpleasant reaction when the patient under treatment ...
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 ... alcohol dehydrogenases. Brewers yeast also has another alcohol dehydrogenase, ADH2, which evolved out of a duplicate version ... Saccharomyces cerevisiae alcohol dehydrogenase 4 (gene ADH4) Zymomonas mobilis alcohol dehydrogenase 2 (gene adhB) Escherichia ... Alcohol dehydrogenases (ADH) (EC 1.1.1.1) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the ...
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. ...
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 ...
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.
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 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 ...
... 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 ...
AcrR and Rex Control Mannitol and Sorbitol Utilization through Their Cross-Regulation of Aldehyde-Alcohol Dehydrogenase (AdhE) ...
  • 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • L2 also possess an alcohol dehydrogenase E (ADHE) that makes them unique among hydrogenosome-bearing anaerobes. (nih.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)
  • 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)
  • In contrast with the report the alcohol dehydrogenase activity in gastric mucosa is lower in women than in men, 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • A known functional SNP in ADH1B (rs1229984) was associated with alcohol intake (P-value = 0.04) but not GC risk. (environment-health.ac.uk)
  • Functional variants in ADH1B and ALDH2 coupled with alcohol and smoking synergistically enhance esophageal cancer risk. (nih.gov)
  • 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)
  • Expression of alcohol dehydrogenase 3 (ADH3) in tissue and cultured cells from human oral mucosa. (springer.com)
  • The retention of the enzyme activity of alcohol dehydrogenase (ADH) has been studied in various drying processes such as spray drying. (mdpi.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)
  • Belongs to the zinc-containing alcohol dehydrogenase family. (abcam.com)
  • Alcohol dehydrogenase derived from yeast is a metalloenzyme containing four tightly bound zinc atoms per molecule (Vallee and Hoch, Proc. (p212121.com)
  • Choose from our alcohol dehydrogenase 7 Peptides and Proteins. (novusbio.com)
  • 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)