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 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 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 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 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 EC 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; EC; EC and EC 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 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 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 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 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 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 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 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 or to a 20-beta-hydroxysteroid (EC 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 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 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 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 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 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.

*  Etanolmetabolismen ur ett alkoholistperspektiv : Kemin vid nedbrytning av etanol i kroppen, dess betydelse för kroppens kemiska...

The study also evaluates the genetic polymorphism of the enzymes alcohol dehydrogenase and aldehyde dehydrogenase, metabolic ... The enzyme alcohol dehydrogenase catalyses the degradation of ethanol to acetaldehyde. Acetaldehyde is even more toxic than ... In chronic alcoholics other chemical processes such as the cytochrome P450 system may have a bigger impact on alcohol ... ethanol and it is degraded by the enzyme aldehyde dehydrogenase. ...

*  Akr1a1 - Alcohol dehydrogenase [NADP(+)] - Mus musculus (Mouse) - Akr1a1 gene & protein

Alcohol dehydrogenase [NADP(+)]Add BLAST. 324. Amino acid modifications. Feature key. Position(s). DescriptionActions. ... alcohol dehydrogenase (NADP+) activity Source: UniProtKB ,p>Non-traceable Author Statement,/p> ,p>Used for statements in the ... sp,Q9JII6,AK1A1_MOUSE Alcohol dehydrogenase [NADP(+)] OS=Mus musculus GN=Akr1a1 PE=1 SV=3 ...

*  KAKEN - Research Projects | Alcohol metabolism in women and hormonal changes. (KAKENHI-PROJECT-07670487)

Alcohol dehydrogenase / Aldehyde dehydrogenase / Gender differences / Estrogen / Testosterone / Alcohol dehydrogenase / ... Blood acetaldehyde levels were influenced by the genotype of aldehyde dehydrogenase 2, but not alcohol dehydrogenase 2. An ... Aldehyde dehydrogenase / Gender difference / Acetal dehyde / Aldebyde dehydrogenase. Research Abstract. Alcohol is more often ... Publications] Eriksson, al.: 'Estrogen-related acetaldehyde elevation in women during alcohol intoxication.' Alcohol. ...

*  BRENDA - aryl-alcohol dehydrogenase

... alcohol dehydrogenase, arylalcohol dehydrogenase, BADH, benzyl alcohol dehydrogenase, CADH II, coniferyl alcohol dehydrogenase ... aryl-alcohol dehydrogenase. This is an abbreviated version, for detailed information about aryl-alcohol dehydrogenase ... Application on EC - aryl-alcohol dehydrogenase. Please wait a moment until all data is loaded. This message will ... An aromatic alcohol. + NAD+. = an aromatic aldehyde. + NADH. + H+. Synonyms. AADH, AC-BADH, ADH, ADP1, ...

*  Anti-Alcohol Dehydrogenase antibody (HRP) - Azide free (ab34575) References

Anti-Alcohol Dehydrogenase antibody (HRP) - Azide free (ab34575) has been cited in 1 publications. Find out more about the ...

*  adf - F420-dependent alcohol dehydrogenase - Methanoculleus thermophilus - adf gene & protein

F420-dependent alcohol dehydrogenaseImported. ,p>Information which has been imported from another database using automatic ... tr,O93734,O93734_9EURY F420-dependent alcohol dehydrogenase (Fragment) OS=Methanoculleus thermophilus GN=adf PE=1 SV=1 ...

*  Computational studies of human class V alcohol dehydrogenase - the odd sibling

... 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 ...

*  Pharmaceutics | Free Full-Text | Encapsulation of Alcohol Dehydrogenase in Mannitol by Spray Drying

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. ...

*  Furaldehyde substrate specificity and kinetics of Saccharomyces cerevisiae alcohol dehydrogenase 1 variants

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. ...

*  Protocol specific for alcohol dehydrogenase 1C RNAi (H00000126-R01): Novus Biologicals

Home » Protocol specific for alcohol dehydrogenase 1C RNAi (H00000126-R01). Protocol specific for alcohol dehydrogenase 1C RNAi ...

*  Alcohol dehydrogenase activity and electron transport in living yeast | Biochemical Journal

Alcohol dehydrogenase activity and electron transport in living yeast. H. Ryan. Biochemical Journal Oct 01, 1967, 105 (1) 137- ... Alcohol dehydrogenase activity and electron transport in living yeast Message Subject (Your Name) has forwarded a page to you ...

*  Alcohol dehydrogenase - Wikipedia

Alcohol dehydrogenase (NAD(P)+) Aldehyde dehydrogenase Oxidoreductase Blood alcohol content for rates of metabolism This ... alcohol dehydrogenases. Brewer's 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 are a group of dehydrogenase enzymes that occur in many organisms and facilitate the ...

*  RCSB PDB - 1NXQ: Crystal Structure of R-alcohol dehydrogenase (RADH) (apoenyzme) from Lactobacillus brevis Methods...

The crystal structure of R-specific alcohol dehydrogenase from Lactobacillus brevis suggests the structural basis of its metal ...

*  Alcohol dehydrogenase (quinone) - Wikipedia

Alcohol dehydrogenase (quinone) (EC, type III ADH, membrane associated quinohaemoprotein alcohol dehydrogenase) is an ... "Quinoprotein alcohol dehydrogenase is involved in catabolic acetate production, while NAD-dependent alcohol dehydrogenase in ... "The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from ... Alcohol dehydrogenase (quinone) at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ...

*  Alcohol dehydrogenase (azurin) - Wikipedia

Alcohol dehydrogenase (azurin) (EC, type II quinoprotein alcohol dehydrogenase, quinohaemoprotein ethanol dehydrogenase ... "Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory ... Alcohol dehydrogenase (azurin) at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ... Groen, B.W.; van Kleef, M.A.; Duine, J.A. (1986). "Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas ...

*  Coniferyl-alcohol dehydrogenase - Wikipedia

... a coniferyl-alcohol dehydrogenase (EC 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. ...

*  Alcohol dehydrogenase (nicotinoprotein) - Wikipedia

Alcohol dehydrogenase (nicotinoprotein) (EC, NDMA-dependent alcohol dehydrogenase, nicotinoprotein alcohol ... Alcohol dehydrogenase (nicotinoprotein) at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and ... Piersma, S.R.; Visser, A.J.; de Vries, S.; Duine, J.A. (1998). "Optical spectroscopy of nicotinoprotein alcohol dehydrogenase ... Norin, A.; Piersma, S.R.; Duine, J.A.; Jornvall, H. (2003). "Nicotinoprotein (NAD+ -containing) alcohol dehydrogenase: ...

*  Allyl-alcohol dehydrogenase - Wikipedia

In enzymology, an allyl-alcohol dehydrogenase (EC is an enzyme that catalyzes the chemical reaction allyl alcohol + ... Otsuka K (1958). "Triphosphopyridine nucleotide-allyl and -ethyl alcohol dehydrogenases from Escherichia coli". J. Gen. Appl. ... The systematic name of this enzyme class is allyl-alcohol:NADP+ oxidoreductase. ... NADP+ ⇌ {\displaystyle \rightleftharpoons } acrolein + NADPH + H+ Thus, the two substrates of this enzyme are allyl alcohol and ...

*  Perillyl-alcohol dehydrogenase - Wikipedia

... a perillyl-alcohol dehydrogenase (EC is an enzyme that catalyzes the chemical reaction perillyl alcohol + NAD+ ⇌ {\ ... This enzyme is also called perillyl alcohol dehydrogenase. This enzyme participates in limonene and pinene degradation. Ballal ... "Perillyl alcohol dehydrogenase from a soil pseudomonad". Biochem. Biophys. Res. Commun. 23 (4): 473-8. doi:10.1016/0006-291X(66 ... The systematic name of this enzyme class is perillyl-alcohol:NAD+ oxidoreductase. ...

*  Cinnamyl-alcohol dehydrogenase - Wikipedia

... a cinnamyl-alcohol dehydrogenase (EC is an enzyme that catalyzes the chemical reaction cinnamyl alcohol + NADP+ ⇌ {\ ... Sarni F, Grand C, Boudet AM (1984). "Purification and properties of cinnamoyl-CoA reductase and cinnamyl alcohol dehydrogenase ... Further studies on cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures". Eur. J. Biochem. 97 (2): 503-9. doi: ... Wyrambik D, Grisebach H (1975). "Purification and properties of isoenzymes of cinnamyl-alcohol dehydrogenase from soybean-cell- ...

*  Alcohol dehydrogenase (acceptor) - Wikipedia

... quinohemoprotein alcohol dehydrogenase, quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase, and alcohol:( ... Alcohol dehydrogenase Ameyama M; Adachi O (1982). "Alcohol dehydrogenase from acetic acid bacteria, membrane-bound". Methods in ... an alcohol dehydrogenase (acceptor) (EC is an enzyme that catalyzes the chemical reaction a primary alcohol + ... Salisbury SA, Forrest HS, Cruse WB, Kennard O (1979). "A novel coenzyme from bacterial primary alcohol dehydrogenases". Nature ...

*  Aryl-alcohol dehydrogenase - Wikipedia

Other names in common use include p-hydroxybenzyl alcohol dehydrogenase, benzyl alcohol dehydrogenase, and coniferyl alcohol ... an aryl-alcohol dehydrogenase (EC is an enzyme that catalyzes the chemical reaction an aromatic alcohol + NAD+ ⇌ {\ ... "Identification and characterization of a nicotinamide adenine dinucleotide-dependent para-hydroxybenzyl alcohol-dehydrogenase ... Suhara K, Takemori S, Katagiri M (1969). "The purification and properties of benzylalcohol dehydrogenase from Pseudomonas sp". ...

*  Alcohol Dehydrogenase | Protein | P212121 Store

Alcohol Dehydrogenase Details. Alcohol dehydrogenase derived from yeast is a metalloenzyme containing four tightly bound zinc ... Click the button below to add the Alcohol Dehydrogenase 100MG to your wish list. ...

*  Cyclic alcohol dehydrogenase (quinone) - Wikipedia

Cyclic alcohol dehydrogenase (quinone) (EC, cyclic alcohol dehydrogenase, MCAD) is an enzyme with systematic name ... Cyclic alcohol dehydrogenase (quinone) at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and ... "Purification and characterization of membrane-bound quinoprotein cyclic alcohol dehydrogenase from Gluconobacter frateurii CHM ... This enzyme catalyses the following chemical reaction cyclic alcohol + quinone ⇌ {\displaystyle \rightleftharpoons } cyclic ...

*  Recently Updated - Reece's Rainbow Down Syndrome Adoption Grant Foundation

This 4 years old girl has been diagnosed with PDD - Pyruvate dehydrogenase deficiency (PDD), Spastic quadriplegia with axial ... Fetal alcohol syndrome, dysmorphia and drooping eyelids. Listed: January 29, 2016. Kaiden has typical FAS, deficiency of weight ... She has rehabilitation every day and is on a special Pyruvate dehydrogenase diet due to the PDD. ...

Alcohol dehydrogenaseAlcohol and cardiovascular disease: Excessive alcohol intake is associated with an elevated risk of alcoholic liver disease (ALD), heart failure, some cancers, and accidental injury, and is a leading cause of preventable death in industrialized countries. However, extensive research has shown that moderate alcohol intake is associated with health benefits, including less cardiovascular disease, diabetes, hypertension, and lower all-cause mortality.Primary alcoholEthanol fuel: Ethanol fuel is ethanol (ethyl alcohol), the same type of alcohol found in alcoholic beverages. It is most often used as a motor fuel, mainly as a biofuel additive for gasoline.Lactate dehydrogenase elevating virus: Lactate dehydrogenase elevating virus, or LDV for short, belongs to part of the arteriviridae family and the nidovirales order. Also included in the nidovirales order are the coronaviridae.Long-chain-aldehyde dehydrogenase: Fatty aldehyde dehydrogenase (or Long-chain-aldehyde dehydrogenase) is an aldehyde dehydrogenase enzyme that in human is encoded in the ALDH3A2 gene on chromosome 17.Sorbitol dehydrogenase: Sorbitol dehydrogenase (or SDH) is a cytosolic enzyme. In humans this protein is encoded by the SORD gene.Prokaryotic acetaldehyde dehydrogenase dimerisation domain: In molecular biology, prokaryotic acetaldehyde dehydrogenase dimerisation domain is a protein domain found at the C-terminus of prokaryotic acetaldehyde dehydrogenases, it adopts a structure consisting of an alpha-beta-alpha-beta(3) core, which mediates dimerisation of the protein.Canadian Thoroughbred Horse Society: The Canadian Thoroughbred Horse Society (CTHS) is an organization headquartered in Toronto, Canada that was founded in 1906 to assist Thoroughbred horse breeders. Since 1982, there have been provincial divisions in Alberta, British Columbia, Manitoba, Ontario, Quebec and Saskatchewan.Dehydrogenase: A dehydrogenase (also called DHO in the literature) is an enzyme belonging to the group of oxidoreductases that oxidizes a substrate by a reduction reaction that transfers one or more hydrides (H−) to an electron acceptor, usually NAD+/NADP+ or a flavin coenzyme such as FAD or FMN.Glutamate dehydrogenase: Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle.Burst kinetics: Burst kinetics is a form of enzyme kinetics that refers to an initial high velocity of enzymatic turnover when adding enzyme to substrate. This initial period of high velocity product formation is referred to as the "Burst Phase".Isocitric acidVanillyl alcoholIsobutanolLiver sinusoid: A liver sinusoid is a type of sinusoidal blood vessel (with fenestrated, discontinuous endothelium) that serves as a location for the oxygen-rich blood from the hepatic artery and the nutrient-rich blood from the portal vein.SIU SOM Histology GIColes PhillipsResearch Society on Alcoholism: The Research Society on Alcoholism (RSA) is a learned society of over 1600 active members based in Austin, Texas. Its objective is to advance research on alcoholism and the physiological and cognitive effects of alcohol.Protein primary structure: The primary structure of a peptide or protein is the linear sequence of its amino acid structural units, and partly comprises its overall biomolecular structure. By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end.Isozyme: Isozymes (also known as isoenzymes or more generally as Multiple forms of enzymes) are enzymes that differ in amino acid sequence but catalyze the same chemical reaction. These enzymes usually display different kinetic parameters (e.Specificity constant: In the field of biochemistry, the specificity constant (also called kinetic efficiency or k_{cat}/K_{M}), is a measure of how efficiently an enzyme converts substrates into products. A comparison of specificity constants can also be used as a measure of the preference of an enzyme for different substrates (i.Glycerol phosphate shuttle: 380px|thumb|Glycerol Phosphate ShuttleDihydrolipoamideSuccinate dehydrogenase subunit E: In molecular biology, the protein domain named Sdh5 is also named SdhE which stands for succinate dehydrogenase protein E. In the past, it has also been named YgfY and DUF339.Cofactor Engineering: Cofactor engineering, a subset of metabolic engineering, is defined as the manipulation of the use of cofactors in an organism’s metabolic pathways. In cofactor engineering, the concentrations of cofactors are changed in order to maximize or minimize metabolic fluxes.Table of standard reduction potentials for half-reactions important in biochemistry: The values below are standard reduction potentials for half-reactions measured at 25°C, 1 atmosphere and a pH of 7 in aqueous solution.Hydroxysteroid dehydrogenaseNitrobenzaldehyde: Nitrobenzaldehyde may refer to any of the three isomeric chemical compounds :Fatty aldehyde: A fatty aldehyde is an aldehyde with a "fatty" aliphatic carbon chain attached that is typically eight carbon or more in length. In contrast, phenolic aldehydes are aromatic.Soluble quinoprotein glucose dehydrogenase: Soluble quinoprotein glucose dehydrogenase (, soluble glucose dehydrogenase, sGDH, glucose dehydrogenase (PQQ-dependent)) is an enzyme with system name D-glucose:acceptor oxidoreductase. This enzyme catalyses the following chemical reactionSymmetry element: A symmetry element is a point of reference about which symmetry operations can take place. In particular, symmetry elements can be centers of inversion, axes of rotation and mirror planes.Glucose-methanol-choline oxidoreductase family: In molecular biology, the glucose-methanol-choline oxidoreductase family (GMC oxidoreductase) is a family of enzymes with oxidoreductase activity.Ligation-independent cloning: Ligation-independent cloning (LIC) is a form of molecular cloning that is able to be performed without the use of restriction endonucleases or DNA ligase. This allows genes that have restriction sites to be cloned without worry of chopping up the insert.SucA RNA motifMannitolDehydratase: Dehydratase is an enzyme that catalyzes the removal of oxygen and hydrogen from organic compounds in the form of water. This process is also known as dehydration reaction.Methoxide: Methoxides are organic salts and the simplest alkoxides. Sodium methoxide and potassium methoxide have widespread use, though other metal-cation variants such as lithium methoxide, rubidium methoxide, caesium methoxide, and francium methoxide exist as well.Phosphogluconate dehydrogenaseSobrietol: Sobrietol is a North American brand of nutritional supplement marketed as a remedy for hangovers and to prevent symptoms associated with alcohol flush reaction. The list of ingredients includes the enzymes quinoptotein alcohol dehydrogenase (QADH) and quinoprotein aldehyde dehydrogenase (QALDH) from Glucanobacter suboxydans or Acetobacter suboxydans or oxydans, either in purified form or as cell extracts, together with buffering agents and protectants designed to ensure that the enzymes remain biologically active after oral ingestion, and "a source of oxygen in an amount sufficient for the enzymes to metabolize ethanol after administration to a patient.NADH dehydrogenase: NADH dehydrogenase (, cytochrome c reductase, type 1 dehydrogenase, beta-NADH dehydrogenase dinucleotide, diaphorase, dihydrocodehydrogenase I dehydrogenase, dihydronicotinamide adenine dinucleotide dehydrogenase, diphosphopyridine diaphorase, DPNH diaphorase, NADH diaphorase, NADH hydrogenase, NADH oxidoreductase, NADH-menadione oxidoreductase, reduced diphosphopyridine nucleotide diaphorase) is an enzyme with systematic name NADH:acceptor oxidoreductase. This enzyme catalyses the following chemical reactionHexafluoro-2-propanolIMP dehydrogenaseAlkaliphile: Alkaliphiles are a class of extremophilic microbes capable of survival in alkaline (pH roughly 8.5-11) environments, growing optimally around a pH of 10.Pyrroloquinoline quinoneAlcohol intoxicationDNA binding site: DNA binding sites are a type of binding site found in DNA where other molecules may bind. DNA binding sites are distinct from other binding sites in that (1) they are part of a DNA sequence (e.Formate dehydrogenase (acceptor): Formate dehydrogenase (acceptor) (, FDHH, FDH-H, FDH-O, formate dehydrogenase H, formate dehydrogenase O) is an enzyme with system name formate:acceptor oxidoreductase. This enzyme catalyses the following chemical reactionMedium-chain acyl-coenzyme A dehydrogenase deficiencyXanthinuriaZinc toxicityPyruvate decarboxylase: Pyruvate decarboxylase is a homotetrameric enzyme () that catalyses the decarboxylation of pyruvic acid to acetaldehyde and carbon dioxide in the cytoplasm of prokaryotes, and in the cytoplasm and mitochondria of eukaryotes. It is also called 2-oxo-acid carboxylase, alpha-ketoacid carboxylase, and pyruvic decarboxylase.Thermoanaerobacter ethanolicus: Thermoanaerobacter ethanolicus is a species of thermophilic, anaerobic, non-spore-forming bacteria.Lactic acid fermentationSterling Clarren: Sterling K. Clarren is one of the world's leading researchers into Fetal Alcohol Spectrum Disorder (FASD), an umbrella term encompassing fetal alcohol syndrome (FAS), alcohol-related neurodevelopmental disorder, static encephalopathy:alcohol exposed and penatal alcohol exposed.List of strains of Escherichia coli: Escherichia coli is a well studied bacterium that was first identified by Theodor Escherich, after whom it was later named.Blended malt whisky: A blended malt, formerly called a vatted malt, or pure malt, is a blend of different single malt whiskies from different distilleries. These terms are most commonly used in reference to Scotch whisky, or whisky in that style, such as Japanese whisky.Fresno County Public LibraryAcid catalysis: In acid catalysis and base catalysis a chemical reaction is catalyzed by an acid or a base. The acid is the proton donor and the base is the proton acceptor.Coniferyl aldehydeA-1,4-glucan-protein synthase (UDP-forming): Alpha-1,4-glucan-protein synthase (UDP-forming) (, UDP-glucose:protein glucosyltransferase, glycogen initiator synthase, UDPGlc:protein transglucosylase, UPTG, uridine diphosphoglucose protein transglucosylase I, proglycogen synthase, uridine diphosphoglucose-protein 4-alpha-glucosyltransferase, uridine diphosphoglucose-protein glucosyltransferase, UDP-glucose protein transglucosylase, UDP-glucose-protein glucosyltransferase, uridine diphosphate glucose-protein transglucosylase I) is an enzyme with system name UDP-glucose:protein 4-alpha-glucosyltransferase. This enzyme catalyses the following chemical reactionFluorouracilMapracoratAdolf Karl Ludwig ClausDatabase of protein conformational diversity: The Database of protein conformational diversity (PCDB) is a database of diversity of protein tertiary structures within protein domains as determined by X-ray crystallography. Proteins are inherently flexible and this database collects information on this subject for use in molecular research.Sharpless asymmetric dihydroxylation: Sharpless asymmetric dihydroxylation (also called the Sharpless bishydroxylation) is the chemical reaction of an alkene with osmium tetroxide in the presence of a chiral quinine ligand to form a vicinal diol.Pseudomonas alkanolytica: Pseudomonas alkanolytica is a Gram-negative soil bacterium that produces Coenzyme A. Because this organism is patented,Nakao Y, Kuno M.Molar mass distribution: In linear polymers the individual polymer chains rarely have exactly the same degree of polymerization and molar mass, and there is always a distribution around an average value. The molar mass distribution (or molecular weight distribution) in a polymer describes the relationship between the number of moles of each polymer species (Ni) and the molar mass (Mi) of that species.Indy (gene): Indy, short for I'm not dead yet, is a gene of the model organism, the fruit fly Drosophila melanogaster. Mutant versions of this gene have doubled the average life span of fruit flies in at least one set of experiments, but this result has been subject to controversy.Zuotin: Z-DNA binding protein 1, also known as Zuotin, is a Saccharomyces cerevisiae yeast gene.Silent mutation: Silent mutations are mutations in DNA that do not significantly alter the phenotype of the organism in which they occur. Silent mutations can occur in non-coding regions (outside of genes or within introns), or they may occur within exons.

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

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)

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

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)

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

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)

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

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)

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

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)

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

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)

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

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)

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

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)


  • In enzymology, a coniferyl-alcohol dehydrogenase (EC 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+. (
  • In enzymology, an alcohol dehydrogenase [NAD(P)+] (EC is an enzyme that catalyzes the chemical reaction an alcohol + NAD(P)+ ⇌ {\displaystyle \rightleftharpoons } an aldehyde + NAD(P)H + H+ The 3 substrates of this enzyme are alcohol, NAD+, and NADP+, whereas its 4 products are aldehyde, NADH, NADPH, and H+. (

liver alcohol dehyd

  • This result gives a third type of evidence, based on purifications and enzyme characterization in lower vertebrates, that the classical liver alcohol dehydrogenase originated by a gene duplication early in the evolution of vertebrates. (
  • The structures of the horse liver alcohol dehydrogenase in various complexes and crystal forms have been determined. (
  • Rotation and translation searches carried out with the programs MERLOT, X-PLOR, GLRF and ALMN in the CCP4 suite with the subunit or domains of horse liver alcohol dehydrogenase have failed to provide a solution consistent with the packing requirements in the unit cell.Work is underway to prepare heavy-atom derivatives. (


  • Alcohol dehydrogenase (quinone) (EC, type III ADH, membrane associated quinohaemoprotein alcohol dehydrogenase) is an enzyme with systematic name alcohol:quinone oxidoreductase. (
  • Alcohol dehydrogenase (azurin) (EC, type II quinoprotein alcohol dehydrogenase, quinohaemoprotein ethanol dehydrogenase, QHEDH, ADHIIB) is an enzyme with systematic name alcohol:azurin oxidoreductase. (
  • The systematic name of this enzyme class is coniferyl-alcohol:NADP+ oxidoreductase. (
  • Alcohol dehydrogenase (nicotinoprotein) (EC, NDMA-dependent alcohol dehydrogenase, nicotinoprotein alcohol dehydrogenase, np-ADH, ethanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase) is an enzyme with systematic name ethanol:acceptor oxidoreductase. (
  • Other names in common use include primary alcohol dehydrogenase, MDH, quinohemoprotein alcohol dehydrogenase, quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase, and alcohol:(acceptor) oxidoreductase. (
  • Cyclic alcohol dehydrogenase (quinone) (EC, cyclic alcohol dehydrogenase, MCAD) is an enzyme with systematic name cyclic alcohol:quinone oxidoreductase. (
  • Polyvinyl alcohol dehydrogenase (cytochrome) (EC, PVA dehydrogenase, PVADH) is an enzyme with systematic name polyvinyl alcohol:ferricytochrome-c oxidoreductase. (
  • Germacrene A alcohol dehydrogenase (EC is an enzyme with systematic name germacra-1(10),4,11(13)-trien-12-ol:NADP+ oxidoreductase. (
  • Alcohol dehydrogenase (cytochrome c) (EC, type I quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase) is an enzyme with systematic name alcohol:cytochrome c oxidoreductase. (
  • Other names in common use include long-chain alcohol dehydrogenase, and fatty alcohol oxidoreductase. (
  • The systematic name of this enzyme class is polyvinyl-alcohol:acceptor oxidoreductase. (
  • Other names in common use include PVA dehydrogenase, and polyvinyl-alcohol:(acceptor) oxidoreductase. (
  • The systematic name of this enzyme class is 3-hydroxybenzyl-alcohol:NADP+ oxidoreductase. (


  • This enzyme catalyses the following chemical reaction primary alcohol + azurin ⇌ {\displaystyle \rightleftharpoons } aldehyde + reduced azurin This enzyme is a periplasmic PQQ-containing quinohemoprotein. (
  • This enzyme catalyses the following chemical reaction cyclic alcohol + quinone ⇌ {\displaystyle \rightleftharpoons } cyclic ketone + quinol This enzyme oxidizes a wide variety of cyclic alcohols. (
  • This enzyme catalyses the following chemical reaction polyvinyl alcohol + ferricytochrome c ⇌ {\displaystyle \rightleftharpoons } oxidized polyvinyl alcohol + ferrocytochrome c + H+ This enzyme participates in bacterial polyvinyl alcohol degradation. (
  • This enzyme catalyses the following chemical reaction a primary alcohol + 2 ferricytochrome c ⇌ {\displaystyle \rightleftharpoons } an aldehyde + 2 ferrocytochrome c + 2 H+ A periplasmic PQQ-containing quinoprotein is present in Pseudomonas and Rhodopseudomonas. (


  • Purification and properties of the alcohol dehydrogenase of Pseudomonas sp. (
  • Existence of a novel enzyme, pyrroloquinoline quinone-dependent polyvinyl alcohol dehydrogenase, in a bacterial symbiont, Pseudomonas sp. (


  • Other names in common use include p-hydroxybenzyl alcohol dehydrogenase, benzyl alcohol dehydrogenase, and coniferyl alcohol dehydrogenase. (
  • Other names in common use include aryl alcohol dehydrogenase (nicotinamide adenine dinucleotide, phosphate), coniferyl alcohol dehydrogenase, NADPH-linked benzaldehyde reductase, and aryl-alcohol dehydrogenase (NADP+). (

cinnamyl-alcohol dehyd

  • Other names in common use include cinnamyl alcohol dehydrogenase, and CAD. (

aryl alcohol

  • This is an abbreviated version, for detailed information about aryl-alcohol dehydrogenase, go to the full flat file . (


  • 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. (
  • Alcohol dehydrogenase, iron containing 1 is a protein that in humans is encoded by the ADHFE1 gene. (


  • In humans, sequencing of the ADH1B gene (responsible for production of an alcohol dehydrogenase polypeptide) shows two variants, in which there is an SNP (single nucleotide polymorphism) that leads to either a Histidine or an Arginine residue in the enzyme catalyzing the conversion of ethanol into acetaldehyde. (
  • Cloning and expression of the gene for periplasmic poly(vinyl alcohol) dehydrogenase from Sphingomonas sp. (
  • Particularly, in preferred embodiments, the invention relates to directed engineering of an enzymatic catalytic site of an alcohol dehydrogenase enzyme gene for enhancing enantioselectivity for (S)-enantiomer substrate catalytic activity for providing aryl (S)-enantiomer products in stereomeric excess. (


  • A previously discovered mutant of Saccharomyces cerevisiae alcohol dehydrogenase 1 (Adh1p) was shown to enable a unique NADH-dependent reduction of 5-hydroxymethylfurfural (HMF), a well-known inhibitor of yeast fermentation. (
  • Alcohol dehydrogenases (ADH) (EC 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). (
  • Other names in common use include retinal reductase, aldehyde reductase (NADPH/NADH), and alcohol dehydrogenase [NAD(P)]. This enzyme participates in glycolysis and gluconeogenesis. (
  • 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. (

aldehyde dehydrogenase

  • There is a single major alcohol dehydrogenase (ADH) and a single major aldehyde dehydrogenase (AldDH) in Aspergillus nidulans . (
  • The two main enzymes involved in alcohol metabolism are alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). (


  • Cloning and expression of soluble cytochrome c and its role in polyvinyl alcohol degradation by polyvinyl alcohol-utilizing Sphingopyxis sp. (


  • In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. (
  • Though this feature is not adaptive from an energy point of view, by making alcohol in such high concentrations so that they would be toxic to other organisms, yeast cells could effectively eliminate their competition. (
  • The first-ever isolated alcohol dehydrogenase (ADH) was purified in 1937 from Saccharomyces cerevisiae (brewer's yeast). (
  • Alcohol dehydrogenase derived from yeast is a metalloenzyme containing four tightly bound zinc atoms per molecule (Vallee and Hoch, Proc. (
  • Yeast alcohol dehydrogenase was one of the first enzymes to be purified and crystallized. (


  • The present invention relates to compositions and methods utilizing thermostable and novel alcohol dehydrogenase enzymes for biosynthesizing chiral specific molecules for use as precursor molecules in synthesizing pharmaceutical compounds. (


  • It is interesting that hexagonal leaflets of crystalline alcohol dehydrogenase form in the cells of Saccharomyces cerevisiae or S. carlsbergensis under certain groth conditions. (


  • Four additional variants of alcohol and aldehyde dehydrogenases have been purified and functionally characterized, and their primary structures have been determined. (


  • 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. (
  • The alcohol dehydrogenases comprise a group of several isozymes that catalyse the oxidation of primary and secondary alcohols to aldehydes and ketones, respectively, and also can catalyse the reverse reaction. (
  • 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). (


  • 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. (


  • 10. The nucleic acid sequence of claim 7, wherein said aryl (S)-enantiomer product is selected from the group comprising (S)-4-phenyl-2-butanol, (S)-phenyl-2-butanol, (S)-1-phenyl-2-butanol, (S)-1-phenyl-2-propanol, and (S)-1-phenyl ethyl alcohol. (


  • The results allow conclusions about the structural and evolutionary relationships within the large family of MDR alcohol dehydrogenases from characterizations of the pigeon (Columba livia) and dogfish (Scyliorhinus canicula) major liver alcohol dehydrogenases. (


  • An alcohol + NADP + = an aldehyde + NADPH. (


  • The results of increased alcohol availability led to alcoholism and abuse by those able to acquire it, resulting in lower reproductive fitness. (
  • Because alcohol metabolism can significantly influence drinking behavior and the risk for alcoholism (Yin and Agarwal 2001), it is important to understand how genetic factors influence metabolism. (