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)

*Lactate dehydrogenase

Ethanol is dehydrogenated to acetaldehyde by alcohol dehydrogenase, and further into acetic acid by acetaldehyde dehydrogenase ... Lactate dehydrogenase-A deficiency is caused by a mutation to the LDHA gene, while lactate dehydrogenase-B deficiency is caused ... LDH is measured by the lactate dehydrogenase (LDH) test (also known as the LDH test or lactic acid dehydrogenase test). ... A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. LDH exist in four distinct enzyme classes. ...

*Ethanol metabolism

Aldehyde dehydrogenase is the second enzyme of the major oxidative pathway of alcohol metabolism. Two major liver isoforms of ... The enzyme encoded by this gene is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a ... In human adults, ethanol is oxidized to acetaldehyde using NAD+, mainly via the hepatic enzyme alcohol dehydrogenase IB (class ... Ethanol, an alcohol found in nature and in alcoholic drinks, is metabolized through a complex catabolic metabolic pathway. ...

*ADH1B

Green RF, Stoler JM (2007). "Alcohol dehydrogenase 1B genotype and fetal alcohol syndrome: a HuGE minireview". Am. J. Obstet. ... Alcohol dehydrogenase Aldehyde dehydrogenase GRCh38: Ensembl release 89: ENSG00000196616 - Ensembl, May 2017 "Human PubMed ... gene encoding the human alcohol dehydrogenase beta 3 subunit". Alcohol. Clin. Exp. Res. 13 (4): 594-6. doi:10.1111/j.1530- ... Alcohol dehydrogenase 1B is an enzyme that in humans is encoded by the ADH1B gene. The protein encoded by this gene is a member ...

*Aldose reductase

The alcohol product is formed via a transfer of the pro-R hydride of NADPH to the re face of the substrate's carbonyl carbon. ... The second and last step in the pathway is catalyzed by sorbitol dehydrogenase, which catalyzes the NAD-linked oxidation of ... Following release of the alcohol product, another conformational change occurs (E*•NADP+ → E•NADP+) in order to release NADP+. ... Jedziniak JA, Yates EM, Kinoshita JH (June 1973). "Lens polyol dehydrogenase". Exp. Eye Res. 16 (2): 95-104. doi:10.1016/0014- ...

*ADH4

This gene encodes class II alcohol dehydrogenase 4 pi subunit, which is a member of the alcohol dehydrogenase family. Members ... 2004). "Alcohol dehydrogenase polymorphisms influence alcohol-elimination rates in a male Jewish population". Alcohol. Clin. ... 2002). "Kinetic mechanism of human class IV alcohol dehydrogenase functioning as retinol dehydrogenase". J. Biol. Chem. 277 (28 ... Class II alcohol dehydrogenase is a homodimer composed of 2 pi subunits. It exhibits a high activity for oxidation of long- ...

*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 1.1.1.1) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the ...

*Alcohol dehydrogenase (quinone)

... (EC 1.1.5.5, type III ADH, membrane associated quinohaemoprotein alcohol dehydrogenase) is an ... "Quinoprotein alcohol dehydrogenase is involved in catabolic acetate production, while NAD-dependent alcohol dehydrogenase in ... "The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from ... Alcohol dehydrogenase (quinone) at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ...

*Alcohol dehydrogenase (azurin)

... (EC 1.1.9.1, type II quinoprotein alcohol dehydrogenase, quinohaemoprotein ethanol dehydrogenase ... "Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory ... 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

... 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. ...

*Alcohol dehydrogenase (nicotinoprotein)

... (EC 1.1.99.36, 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

In enzymology, an allyl-alcohol dehydrogenase (EC 1.1.1.54) is an enzyme that catalyzes the chemical reaction allyl alcohol + ... Otsuka K (1958). "Triphosphopyridine nucleotide-allyl and -ethyl alcohol dehydrogenases from Escherichia coli". J. Gen. Appl. ... The systematic name of this enzyme class is allyl-alcohol:NADP+ oxidoreductase. ... NADP+ ⇌ {\displaystyle \rightleftharpoons } acrolein + NADPH + H+ Thus, the two substrates of this enzyme are allyl alcohol and ...

*Perillyl-alcohol dehydrogenase

... a perillyl-alcohol dehydrogenase (EC 1.1.1.144) is an enzyme that catalyzes the chemical reaction perillyl alcohol + NAD+ ⇌ {\ ... This enzyme is also called perillyl alcohol dehydrogenase. This enzyme participates in limonene and pinene degradation. Ballal ... "Perillyl alcohol dehydrogenase from a soil pseudomonad". Biochem. Biophys. Res. Commun. 23 (4): 473-8. doi:10.1016/0006-291X(66 ... The systematic name of this enzyme class is perillyl-alcohol:NAD+ oxidoreductase. ...

*Cinnamyl-alcohol dehydrogenase

... a cinnamyl-alcohol dehydrogenase (EC 1.1.1.195) is an enzyme that catalyzes the chemical reaction cinnamyl alcohol + NADP+ ⇌ {\ ... Sarni F, Grand C, Boudet AM (1984). "Purification and properties of cinnamoyl-CoA reductase and cinnamyl alcohol dehydrogenase ... Further studies on cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures". Eur. J. Biochem. 97 (2): 503-9. doi: ... Wyrambik D, Grisebach H (1975). "Purification and properties of isoenzymes of cinnamyl-alcohol dehydrogenase from soybean-cell- ...

*Alcohol dehydrogenase (acceptor)

... quinohemoprotein alcohol dehydrogenase, quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase, and alcohol:( ... Alcohol dehydrogenase Ameyama M; Adachi O (1982). "Alcohol dehydrogenase from acetic acid bacteria, membrane-bound". Methods in ... an alcohol dehydrogenase (acceptor) (EC 1.1.99.8) is an enzyme that catalyzes the chemical reaction a primary alcohol + ... Salisbury SA, Forrest HS, Cruse WB, Kennard O (1979). "A novel coenzyme from bacterial primary alcohol dehydrogenases". Nature ...

*Aryl-alcohol dehydrogenase

Other names in common use include p-hydroxybenzyl alcohol dehydrogenase, benzyl alcohol dehydrogenase, and coniferyl alcohol ... an aryl-alcohol dehydrogenase (EC 1.1.1.90) is an enzyme that catalyzes the chemical reaction an aromatic alcohol + NAD+ ⇌ {\ ... "Identification and characterization of a nicotinamide adenine dinucleotide-dependent para-hydroxybenzyl alcohol-dehydrogenase ... Suhara K, Takemori S, Katagiri M (1969). "The purification and properties of benzylalcohol dehydrogenase from Pseudomonas sp". ...

*Cyclic alcohol dehydrogenase (quinone)

... (EC 1.1.5.7, 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 ...

*Polyvinyl alcohol dehydrogenase (cytochrome)

... vinyl alcohol) dehydrogenase from Sphingomonas sp. strain 113P3, a novel-type quinohaemoprotein alcohol dehydrogenase". ... Polyvinyl alcohol dehydrogenase (cytochrome) (EC 1.1.2.6, PVA dehydrogenase, PVADH) is an enzyme with systematic name polyvinyl ... Polyvinyl alcohol dehydrogenase (cytochrome) at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular ... pyrroloquinoline quinone-dependent polyvinyl alcohol dehydrogenase, in a bacterial symbiont, Pseudomonas sp. strain VM15C". ...

*Germacrene A alcohol dehydrogenase

... (EC 1.1.1.314) is an enzyme with systematic name germacra-1(10),4,11(13)-trien-12-ol:NADP+ ... Germacrene A alcohol dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and ... Demonstration of a cytochrome P450 (+)-germacrene A hydroxylase and NADP+-dependent sesquiterpenoid dehydrogenase(s) involved ...

*Alcohol dehydrogenase (cytochrome c)

... (EC 1.1.2.8, type I quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase ... Alcohol dehydrogenase (cytochrome c) at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and ... "Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols". J. ... Mennenga, B.; Kay, C.W.; Gorisch, H. (2009). "Quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: the unusual ...

*Long-chain-alcohol dehydrogenase

Other names in common use include long-chain alcohol dehydrogenase, and fatty alcohol oxidoreductase. This enzyme participates ... a long-chain-alcohol dehydrogenase (EC 1.1.1.192) is an enzyme that catalyzes the chemical reaction a long-chain alcohol + 2 ... Lee T (1979). "Characterization of fatty alcohol:NAD+ oxidoreductase from rat liver". J. Biol. Chem. 254 (8): 2892-6. PMID ... The systematic name of this enzyme class is long-chain-alcohol:NAD+ oxidoreductase. ...

*Polyvinyl-alcohol dehydrogenase (acceptor)

... a polyvinyl-alcohol dehydrogenase (acceptor) (EC 1.1.99.23) is an enzyme that catalyzes the chemical reaction polyvinyl alcohol ... Other names in common use include PVA dehydrogenase, and polyvinyl-alcohol:(acceptor) oxidoreductase. It employs one cofactor, ... pyrroloquinoline quinone-dependent polyvinyl alcohol dehydrogenase, in a bacterial symbiont, Pseudomonas sp. strain VM15C". ... the two substrates of this enzyme are polyvinyl alcohol and acceptor, whereas its two products are oxidized polyvinyl alcohol ...

*Aryl-alcohol dehydrogenase (NADP+)

... coniferyl alcohol dehydrogenase, NADPH-linked benzaldehyde reductase, and aryl-alcohol dehydrogenase (NADP+). Gross GG, Zenk MH ... an aryl-alcohol dehydrogenase (NADP+) (EC 1.1.1.91) is an enzyme that catalyzes the chemical reaction an aromatic alcohol + ... Other names in common use include aryl alcohol dehydrogenase (nicotinamide adenine dinucleotide, phosphate), ... 2. Purification and properties of aryl-alcohol: NADP-oxidoreductase from Neurospora crassa]". Eur. J. Biochem. (in German). 8 ( ...

*3-hydroxybenzyl-alcohol dehydrogenase

Other names in common use include m-hydroxybenzyl alcohol dehydrogenase, m-hydroxybenzyl alcohol (NADP+) dehydrogenase, and m- ... a 3-hydroxybenzyl-alcohol dehydrogenase (EC 1.1.1.97) is an enzyme that catalyzes the chemical reaction 3-hydroxybenzyl alcohol ... Forrester PI, Gaucher GM (1972). "m-Hydroxybenzyl alcohol dehydrogenase from Penicillium urticae". Biochemistry. 11 (6): 1108- ... The systematic name of this enzyme class is 3-hydroxybenzyl-alcohol:NADP+ oxidoreductase. ...

*Alcohol dehydrogenase (NAD(P)+)

... and alcohol dehydrogenase [NAD(P)]. This enzyme participates in glycolysis and gluconeogenesis. Alcohol dehydrogenase Fidge NH ... In enzymology, an alcohol dehydrogenase [NAD(P)+] (EC 1.1.1.71) is an enzyme that catalyzes the chemical reaction an alcohol + ... The systematic name of this enzyme class is alcohol:NAD(P)+ oxidoreductase. Other names in common use include retinal reductase ... NAD(P)+ ⇌ {\displaystyle \rightleftharpoons } an aldehyde + NAD(P)H + H+ The 3 substrates of this enzyme are alcohol, NAD+, and ...

*Alcohol dehydrogenase, iron containing 1

... is a protein that in humans is encoded by the ADHFE1 gene. The ADHFE1 gene encodes ... Alcohol dehydrogenase, iron containing 1". Retrieved 2017-06-16. Kardon T, Noël G, Vertommen D, Schaftingen EV (April 2006). " ... "Alcohol dehydrogenase, iron containing, 1 promoter hypermethylation associated with colorectal cancer differentiation". BMC ... "Cloning and characterization of a novel human alcohol dehydrogenase gene (ADHFe1)". DNA Sequence. 13 (5): 301-6. doi:10.1080/ ...

*Metabolism

The acyl chains in the fatty acids are extended by a cycle of reactions that add the acyl group, reduce it to an alcohol, ... Hundreds of separate types of dehydrogenases remove electrons from their substrates and reduce NAD+ into NADH. This reduced ... In the 19th century, when studying the fermentation of sugar to alcohol by yeast, Louis Pasteur concluded that fermentation was ... In anaerobic conditions, glycolysis produces lactate, through the enzyme lactate dehydrogenase re-oxidizing NADH to NAD+ for re ...

*Gösta Pettersson (biochemist)

... 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). ...
Class I alcohol dehydrogenases (ADH1s) are the rate-limiting enzymes for ethanol and vitamin A (retinol) metabolism in the liver . Because previous studies have shown that human ADH1 enzymes may participate in bile acid metabolism, we investigated whether the bile acid-activated nuclear receptor farnesoid X receptor (FXR) regulates ADH1 genes. In human hepatocytes, both the endogenous FXR ligand chenodeoxycholic acid and synthetic FXR-specific agonist GW4064 increased ADH1 mRNA, protein, and activity. Moreover, overexpression of a constitutively active form of FXR induced ADH1A and ADH1B expression, whereas silencing of FXR abolished the effects of FXR agonists on ADH1 expression and activity. Transient transfection studies and electrophoretic mobility shift assays revealed functional FXR response elements in the ADH1A and ADH1B proximal promoters, thus indicating that both genes are direct targets of FXR. These findings provide the first evidence for direct connection of bile acid signaling and ...
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 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 ...
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. ...
Experimental procedures: Adh constructs were derived from an 8.6-kb SacI-ClaI fragment of the Wa-F allele (Kreitman 1983). Mutagenesis was performed on a pUC18 plasmid containing the 8.6-kb fragment using the Quick-change mutagenesis kit (Stratagene, La Jolla, CA). A single nucleotide substitution was made at codon 16 (CTG to CTA) to create the 1 Leu mutant construct. For the 6 Leu mutant construct, nucleotide substitutions were made at codons 5 (TTG to CTA), 16 (CTG to CTA), 21 (CTG to CTA), 27 (CTG to CTA), 28 (CTC to CTA), and 32 (CTG to CTA). With the exception of codon 5, the 10 Leu mutant construct contained the same substitutions as the 6 Leu construct, with an additional five substitutions at codons 35 (CTG to CTA), 38 (CTC to CTA), 50 (CTG to CTA), 76 (CTG to CTA), and 77 (CTG to CTA). Mutant clones were sequenced to ensure that the desired mutation(s) were present before proceeding. The 8.6-kb SacI-ClaI fragment was subcloned into a ClaI site added to the YES transformation vector ...
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.
Yokoyama, A., Yokoyama, T., Matsui, T., Mizukami, T., Matsushita, S., Higuchi, S. and Maruyama, K. (2013), Alcohol Dehydrogenase-1B Genotype (rs1229984) is a Strong Determinant of the Relationship Between Body Weight and Alcohol Intake in Japanese Alcoholic Men. Alcoholism: Clinical and Experimental Research, 37: 1123-1132. doi: 10.1111/acer.12069 ...
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 ...
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 ...
Dear Arabidopsis researchers, The following information is the number of Arabidopsis entries in GenBank that are new or were updated in the last week. These sequences have been updated in TAIR and are available for searching using TAIR BLAST and FASTA at: http://arabidopsis.org/blast/ http://arabidopsis.org/cgi-bin/fasta/TAIRfasta.pl New sequences : 25 Updated sequences : 0 Updated annotation : 28 ====================== New DNA Sequences ======================= ALY251276 AJ251276 1687bp DNA PLN 09-FEB-2000 Arabidopsis lyrata subsp. petraea partial adh gene for alcohol dehydrogenase, exons 1-7 Kar-26 ADH gene; alcohol dehydrogenase; adh. ALY251277 AJ251277 1683bp DNA PLN 09-FEB-2000 Arabidopsis lyrata subsp. petraea partial adh gene for alcohol dehydrogenase, exons 1-7 Kar-8 ADH gene; alcohol dehydrogenase; adh. ALY251278 AJ251278 1688bp DNA PLN 09-FEB-2000 Arabidopsis lyrata subsp. petraea partial adh gene for alcohol dehydrogenase, exons 1-7 Kar-12 ADH gene; alcohol dehydrogenase; adh. ...
cytosol, extracellular exosome, alcohol dehydrogenase (NAD) activity, alcohol dehydrogenase activity, zinc-dependent, zinc ion binding, ethanol oxidation, response to ethanol
The three-dimensional structure of the human beta3beta3 dimeric alcohol dehydrogenase (beta3) was determined to 2.4-A resolution. beta3 was crystallized as a ternary complex with the coenzyme NAD+ and the competitive inhibitor 4-iodopyrazole. beta3 is a polymorphic variant at ADH2 that differs from beta1 by a single amino acid substitution of Arg-369 --, Cys. The available x-ray structures of mammalian alcohol dehydrogenases show that the side chain of Arg-369 forms an ion pair with the NAD(H) pyrophosphate to stabilize the E.NAD(H) complex. The Cys-369 side chain of beta3 cannot form this interaction. The three-dimensional structures of beta3 and beta1 are virtually identical, with the exception that Cys-369 and two water molecules in beta3 occupy the position of Arg-369 in beta1. The two waters occupy the same positions as two guanidino nitrogens of Arg-369. Hence, the number of hydrogen bonding interactions between the enzyme and NAD(H) are the same for both isoenzymes. However, beta3 differs ...
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 ...
References for Abcams Recombinant Human ADH5 protein (ab124573). Please let us know if you have used this product in your publication
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 ...
Sequence variation of alcohol dehydrogenase (Adh) paralogs in cactophilic Drosophila.: This study focuses on the population genetics of alcohol dehydrogenase (A
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
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 ...
Álcool desidrogenase 4 é uma enzima que nos humanos é codificada pelo gene ADH4. Este gene codifica a subunidade pi da álcool desidrogenase 4 classe II, que é um dos membros da família das álcool desidrogenases. Os membros desta família de enzimas metabolizam uma grande variedade de substratos, incluindo etanol, retinol, outros álcoois alifáticos, hidroesteróides e produtos da peroxidação lipídica. A álcool desidrogenase 4 de classe II é um homodímero composto de duas subunidades pi. Exibe uma actividade alta para oxidação de álcoois alifáticos de cadeia longa e álcoois aromáticos e é menos sensível ao pirazol. Este gene está localizado no cromossoma 4, no cluster de genes da álcool desidrogenase. «Entrez Gene: ADH4 alcohol dehydrogenase 4 (class II), pi polypeptide» Jörnvall H (1994). «The alcohol dehydrogenase system.». EXS. 71: 221-9. PMID 8032153 Edman K, Maret W (1993). «Alcohol dehydrogenase genes: restriction fragment length polymorphisms for ADH4 (pi-ADH) ...
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 effect of the alcohol dehydrogenase locus (Adh) on various life history traits in Drosophila mercatorum is discussed with respect to their potential ability to maintain polymorphism. In particular, developmental time, viability and fecundity are studied in different conditions to determine the impact of environmental change on these traits.
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 ...
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 ...
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.. ...
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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, ...
Pharmacokinetics. Bosron WF, Ehrig T, Li T-K. Genetic factors in alcohol metabolism and alcoholism. Semin Liver Dis 13:126-135 (1993).. Chen CC, Lu RB, Chen YC, Wang MF, Chang YC, Li T-K, Yin SJ. Interaction between the functional polymorphisms of the alcohol-metabolism genes in protection against alcoholism. Am J Human Genet 65:795-807 (1999).. Dubowski KM. Absorption, distribution and elimination of alcohol: Highway safety aspects. J Stud Alcohol Suppl 10:98-108 (1985).. Holford NHG. Clinical pharmacokinetics of ethanol. Clin Pharmacokinet 13:273-292 (1987).. Li T-K, Beard JD, Orr WE, Kwo PY, Ramchandani VA, Thomasson HR. Variation in ethanol pharmacokinetics and perceived gender and ethnic differences. Alcohol Clin Exp Res 24:415-416 (2000).. McCarver DG, Thomasson HR, Martier SS, Sokol RJ, Li T-K. Alcohol dehydrogenase-2*3 allele protects against alcohol-related birth defects among African-Americans. J Pharmacol Exp Ther 283:1095-1101 (1997).. Mumenthaler MS, Taylor JL, OHara R, Yesavage ...
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 ...
Similar to Dehydrogenase/reductase SDR family member 4 (EC 1.1.1.184) (NADPH- dependent carbonyl reductase/NADP-retinol dehydrogenase) (CR) (PHCR) (Peroxisomal short-chain alcohol dehydrogenase) (NADPH-dependent retinol dehydrogenase/reductase) (NDRD) (SCAD-SRL) (humNRDR) (PSCD). Splice isoform 2 ...
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).
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
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Background The rapid growth of protein-protein interaction (PPI) data has led to the emergence of PPI network analysis. from POINT http://point.bioinformatics.tw/ and POINeT http://poinet.bioinformatics.tw/. Further development of methods to forecast host-pathogen relationships should incorporate multiple methods in order to improve level of sensitivity, and should facilitate the recognition of focuses on for drug finding and … Continue reading Background The rapid growth of protein-protein interaction (PPI) data has led. ...
tr:A0A0F6BSE2_GEOS0] Alcohol dehydrogenase GroES domain protein; K13953 alcohol dehydrogenase, propanol-preferring [EC:1.1.1.1] ...
Mouse polyclonal antibody raised against a full-length human ADH1C protein. ADH1C (NP_000660.1, 1 a.a. ~ 375 a.a) full-length human protein. (H00000126-B01P) - Products - Abnova
Human ADH4 full-length ORF ( AAH22319.1, 1 a.a. - 380 a.a.) recombinant protein with GST-tag at N-terminal. (H00000127-P01) - Products - Abnova
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Complete information for ADH4 gene (Protein Coding), Alcohol Dehydrogenase 4 (Class II), Pi Polypeptide, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for ADH6 gene (Protein Coding), Alcohol Dehydrogenase 6 (Class V), including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Dear Network Can anyone provide me with the sequence of the ADH gene from Columbia or else a clone that I could sequence? Only the Landsberg sequence is in the databank. Thanks Uschi Hanfstingl Dept.of Molecular Biology Mass.General Hospital Boston, MA 02114 ...
Principal Investigator:FUKUNAGA Tatsushige, Project Period (FY):1995 - 1996, Research Category:Grant-in-Aid for Scientific Research (C), Section:一般, Research Field:Legal medicine
CRYSTALLIZATION OF HUMAN BETA1 ALCOHOL DEHYDROGENASE (15 MG/ML) IN 50 MM SODIUM PHOSPHATE (PH 7.5), 2.0 MM NAD+ AND 1 MM 4-IODOPYRAZOLE AT 25 OC, 13% (W/V) PEG ...
Lets not forget January was a resit paper, so grade boundaries tend to be higher. This paper was decent but a lot of people would have been thrown by the alcohol dehydrogenase question and some others too. Think grade boundaries will be the usual, nothing more nothing less ...
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Umfassende Darstellung von medizinischen Laborparametern. Mehr als die H lfte aller Erkrankungen werden durch Laborparameter entdeckt oder im Verlauf kontrolliert.
Four additional variants of alcohol and aldehyde dehydrogenases have been purified and functionally characterized, and their primary structures have been determined. The results allow conclusions about the structural and evolutionary relationships within the large family of MDR alcohol dehydrogenases from characterizations of the pigeon (Columba livia) and dogfish (Scyliorhinus canicula) major liver alcohol dehydrogenases. The pigeon enzyme turns out to be of class I type and the dogfish enzyme of class III type. This result gives a third type of evidence, based on purifications and enzyme characterization in lower vertebrates, that the classical liver alcohol dehydrogenase originated by a gene duplication early in the evolution of vertebrates. It is discernable as the major liver form at about the level in-between cartilaginous and osseous fish. The results also show early divergence within the avian orders. Structures were determined by Edman degradations, making it appropriate to acknowledge ...
Heavy alcohol drinking is a risk factor of colorectal cancer (CRC), but little is known on the effect of polymorphisms in the alcohol-metabolizing enzymes, alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) on the alcohol-related risk of C
Looking for online definition of Alcohol metabolism in the Medical Dictionary? Alcohol metabolism explanation free. What is Alcohol metabolism? Meaning of Alcohol metabolism medical term. What does Alcohol metabolism mean?
TY - JOUR. T1 - Influence of temperature on the production of archaeal thermoactive alcohol dehydrogenases from Pyrococcus furiosus with recombinant E. coli. AU - Kube, J.. AU - Brokamp, C.. AU - Machielsen, M.P.. AU - van der Oost, J.. AU - Markl, H.. PY - 2006. Y1 - 2006. N2 - The heterologous production of a thermoactive alcohol dehydrogenase (AdhC) from Pyrococcus furiosus in Escherichia coli was investigated. E. coli was grown in a fed-batch bioreactor in minimal medium to high cell densities (cell dry weight 76 g/l, OD600 of 150). Different cultivation strategies were applied to optimize the production of active AdhC, such as lowering the cultivation temperature from 37 to 28°C, heat shock of the culture from 37 to 42°C and from 37 to 45°C, and variation of time of induction (induction at an OD600 of 40, 80 and 120). In addition to the production of active intracellular protein, inclusion bodies were always observed. The maximal activity of 30 U/l (corresponding to 6 mg/l active ...
Excessive alcohol consumption is associated with spontaneous burning pain, hyperalgesia, and allodynia. Although acetaldehyde has been implicated in the painful alcoholic neuropathy, the mechanism by which the ethanol metabolite causes pain symptoms is unknown. Acute ethanol ingestion caused delayed mechanical allodynia in mice. Inhibition of alcohol dehydrogenase (ADH) or deletion of transient receptor potential ankyrin 1 (TRPA1), a sensor for oxidative and carbonyl stress, prevented allodynia. Acetaldehyde generated by ADH in both liver and Schwann cells surrounding nociceptors was required for TRPA1-induced mechanical allodynia. Plp1-Cre Trpa1fl/fl mice with a tamoxifen-inducible specific deletion of TRPA1 in Schwann cells revealed that channel activation by acetaldehyde in these cells initiates a NADPH oxidase-1-dependent (NOX1-dependent) production of hydrogen peroxide (H2O2) and 4-hydroxynonenal (4-HNE), which sustains allodynia by paracrine targeting of nociceptor TRPA1. Chronic ethanol ...
Excessive alcohol consumption is associated with spontaneous burning pain, hyperalgesia, and allodynia. Although acetaldehyde has been implicated in the painful alcoholic neuropathy, the mechanism by which the ethanol metabolite causes pain symptoms is unknown. Acute ethanol ingestion caused delayed mechanical allodynia in mice. Inhibition of alcohol dehydrogenase (ADH) or deletion of transient receptor potential ankyrin 1 (TRPA1), a sensor for oxidative and carbonyl stress, prevented allodynia. Acetaldehyde generated by ADH in both liver and Schwann cells surrounding nociceptors was required for TRPA1-induced mechanical allodynia. Plp1-Cre Trpa1fl/fl mice with a tamoxifen-inducible specific deletion of TRPA1 in Schwann cells revealed that channel activation by acetaldehyde in these cells initiates a NADPH oxidase-1-dependent (NOX1-dependent) production of hydrogen peroxide (H2O2) and 4-hydroxynonenal (4-HNE), which sustains allodynia by paracrine targeting of nociceptor TRPA1. Chronic ethanol ...
It is the simplest alcohol, and is a light, volatile, colourless, flammable, poisonous liquid with a distinctive odor that is somewhat milder and sweeter than ethanol (Wikipedia). Methanol is responsible for accidental, suicidal, and epidemic poisonings, resulting in death or permanent sequelae. Toxicity is due to the metabolic products of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase. (PMID 15627163 ). The rapid and accurate diagnosis of toxic alcohol poisoning due to methanol (methyl alcohol) is paramount in preventing serious adverse outcomes. The quantitative measurement of specific serum levels of methanol using gas chromatography is expensive, time consuming and generally only available at major tertiary-care facilities. (PMID 15862085 ...
Hyperthermophiles grow optimally at 80 ºC and above, and many of them have the ability to utilize various carbohydrates as carbon source and produce ethanol as an end product. Alcohol dehydrogenase (ADH) is a key enzyme responsible for alcohol production, catalyzing interconversions between alcohols and corresponding ketones or aldehydes. ADHs from hyperthermophiles are of great interests due to their thermostability, high activity and enantioselectivity. The gene encoding ADH from hyperthermophilic archaeon Thermococcus guaymasensis was cloned, sequenced and over-expressed. DNA fragments of the genes encoding the ADHs were amplified directly from the corresponding genomic DNA by combining the use of conventional and inverse PCRs. The entire gene was detected to be 1092 bp and the deduced amino acid sequence had a total of 364 amino acids with a calculated molecular mass of 39463 Dalton. The enzyme belonged to the family of zinc-containing ADHs with catalytic zinc only. It was verified that the ...
Expression of the CTA1 gene of Saccharomyces cerevisiae, encoding catalase A, the peroxisomal catalase of this yeast, is sensitive to glucose repression. A DNA fragment cloned as a multicopy plasmid suppressing the glucose repression of CTA1 transcription was demonstrated to contain the ADR1 gene. Multiple copies of ADR1 increased catalase A formation not only on 10% glucose, but also on ethanol medium and in the presence of oleic acid, an inducer of peroxisome proliferation. Compared with wild-type cells, adr1 null mutants produced by disruption of the gene exhibit reduced CTA1 expression. This demonstrates that ADR1 is a true positive regulator of CTA1. Further experiments showed that it acts directly on CTA1. Alcohol dehydrogenase II, which is under ADR1 control, was excluded as a mediator of the effect on CTA1; deletion of bases -123 to -168 of CTA1 reduces expression and eliminates the response to the ADR1 multicopy plasmid without eliminating fatty acid induction; and gel retardation ...
Genetic linkage studies with alcoholics have provided strong support for the assumption that AA plays a central role in alcohol-associated carcinogenesis. These studies found that individuals who accumulate AA because they carry certain alleles of the genes encoding ADH or ALDH have an increased cancer risk [42, 43]. As discussed above there are at least seven isozymes of human ADH that are encoded by seven genes. These isozymes are categorized into five different classes based on structural characteristics. Class I isozymes account for most of the alcohol metabolism.. For both the ADH1B and the ADH1C genes, several alleles exist that result in differences in the activity of the ADH molecules they encode. For example, the ADH1B*2 allele encodes an enzyme that is approximately 40 times more active than the enzyme encoded by the ADH1B*1 allele. Similarly, the enzyme encoded by the ADH1C*1 allele is 2.5 times more active than the enzyme encoded by the ADH1C*2 allele [44]. Individuals who carry the ...
Reactions of oestrogens and androgens at position C-17 are catalysed by 17 beta-hydroxysteroid dehydrogenases (17 beta-HSDs). Cloning of the cDNA of a novel human 17 beta-HSD IV and expression of its mRNA are described. A probe derived from the recently discovered porcine 17 beta-oestradiol dehydrogenase (17 beta-EDH) was used to isolate a 2.6 kb human cDNA encoding a continuous protein of 736 amino acids of high (84 %) similarity to the porcine 17 beta-EDH. The calculated molecular mass of the human enzyme is 79 595 Da. Other sequence similarities shared by the two enzymes are : an N-terminal sequence which is similar to that of members of the short-chain alcohol dehydrogenase family ; amino acids 343-607 which are similar to the C-terminal domains of a trifunctional Candida tropicalis enzyme and the FOX2 gene product of Saccharomyces cerevisiae ; amino acids 596-736 which are similar to human sterol carrier protein 2. The previously cloned human 17 beta-HSD I, II and III are less than 25% ...
Genetic variants of the alcohol-metabolizing enzyme ADH4, located on chromosome 4q22-4q23, have been related to alcohol dependence (AD) risk in previous research. The aim of this association study in a large multicenter sample of alcohol-dependent individuals and controls is to confirm ADH4 single nucleotide polymorphism (SNP) and haplotype association with AD and relevant related phenotypes. One thousand, six hundred and twenty-two (1622) inpatient subjects and 1469 control subjects with DSM-IV. AD from four addiction treatment centres were included. Characteristics of AD and related phenotypes including alcohol withdrawal, Cloningers type I and II and first ages of drinking, regular drinking and AD onset were obtained using standardized structured interviews. After subjects were genotyped for 2 ADH4 polymorphisms, single SNP case-control and haplotype analyses were conducted. Both variants-rs1800759 and rs1042364-and the A-A and C-G haplotypes were significantly related to AD across samples. ...
One hypothesis for the difference between the sexes is that men have a higher activity of the enzyme ADH, as I mentioned earlier, which metabolizes methanol and converts it to formaldehyde. More formaldehyde circulating in your blood would naturally have more opportunity to cause greater damage. Its possible that there is some hormonally mediated protection against the adverse effects of aspartame in women, in addition to men having higher ADH activity, but the study was not designed to answer that question. All in all however, I believe the study offers significant supporting evidence of the danger that aspartame-sweetened and other "diet" drinks and foods pose ...
51278PRTHomo sapiens 1Met His Lys Ala Gly Leu Leu Gly Leu Cys Ala Arg Ala Trp Asn Ser1 5 10 15Val Arg Met Ala Ser Ser Gly Met Thr Arg Arg Asp Pro Leu Ala Asn20 25 30Lys Val Ala Leu Val Thr Ala Ser Thr Asp Gly Ile Gly Phe Ala Ile35 40 45Ala Arg Arg Leu Ala Gln Asp Gly Ala His Val Val Val Ser Ser Arg50 55 60Lys Gln Gln Asn Val Asp Gln Ala Val Ala Thr Leu Gln Gly Glu Gly65 70 75 80Leu Ser Val Thr Gly Thr Val Cys His Val Gly Lys Ala Glu Asp Arg85 90 95Glu Arg Leu Val Ala Thr Ala Val Lys Leu His Gly Gly Ile Asp Ile100 105 110Leu Val Ser Asn Ala Ala Val Asn Pro Phe Phe Gly Ser Ile Met Asp115 120 125Val Thr Glu Glu Val Trp Asp Lys Thr Leu Asp Ile Asn Val Lys Ala130 135 140Pro Ala Leu Met Thr Lys Ala Val Val Pro Glu Met Glu Lys Arg Gly145 150 155 160Gly Gly Ser Val Val Ile Val Ser Ser Ile Ala Ala Phe Ser Pro Ser165 170 175Pro Gly Phe Ser Pro Tyr Asn Val Ser Lys Thr Ala Leu Leu Gly Leu180 185 190Thr Lys Thr Leu Ala Ile Glu Leu Ala Pro Arg Asn Ile Arg Val Asn195 200 205Cys Leu Ala Pro Gly Leu Ile Lys Thr ...
ID ADHE_ECOLI Reviewed; 891 AA. AC P0A9Q7; P17547; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 22-NOV-2017, entry version 109. DE RecName: Full=Aldehyde-alcohol dehydrogenase; DE Includes: DE RecName: Full=Alcohol dehydrogenase; DE Short=ADH; DE EC=1.1.1.1; DE Includes: DE RecName: Full=Acetaldehyde dehydrogenase [acetylating]; DE Short=ACDH; DE EC=1.2.1.10; DE Includes: DE RecName: Full=Pyruvate-formate-lyase deactivase; DE Short=PFL deactivase; GN Name=adhE; Synonyms=ana; OrderedLocusNames=b1241, JW1228; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11. RX PubMed=2695398; DOI=10.1016/0378-1119(89)90483-6; RA Goodlove P.E., Cunningham P.R., Parker J., Clark D.P.; RT "Cloning and sequence analysis of the fermentative alcohol- RT dehydrogenase-encoding gene of ...
A continuous-flow apparatus is described for automatically plotting substrate saturation curves, and is suitable for use with a variety of enzymes. A linear concentration gradient of the variable substrate is combined with a fixed proportion of the other substrates and the enzyme, and after passing through a reaction coil the product concentrations are measured spectrophotometrically. Use of a 4cm. flow cell and modified spectrophotometer permits accurate measurement of NADH concentration in the region of 0·1μm. Precise control over reaction times and substrate concentration is achieved by using power-driven syringes with an integral mixer. Specimen results are given for yeast alcohol dehydrogenase.. ...
GenBank) aldehyde-alcohol dehydrogenase 2 [Includes: Alcohol dehydrogenase (EC 1.1.1.1) (ADH); Acetaldehyde dehydrogenase (ACDH ...
Scientists have discovered a link between mouth cancer and the rate at which genes break down alcohol.. The genes that regulate how quickly people get drunk also influence their risks of developing cancer of the mouth, larynx or gullet, a new study has found.. Hundreds of patients with cancers of the mouth, larynx and oesophagus in Europe and Central and South America, together with patients free of the disease, were studied by researchers at Aberdeen University.. Two genes involved in metabolising alcohol - a substance already known to be a risk factor for oral cancer - were focused on.. People with a fast-acting variant of the gene for alcohol dehydrogenase - the enzyme that breaks down alcohol - were at much lower risk of these cancers, according to scientists collaborating in the international study.. Researchers found that the reason is these hyper-active enzymes break down alcohol - which is a toxin - more quickly.. This means that the mouth and throat are exposed to the damaging effects ...
Ethanol (alcohol)-mediated cell and tissue damage is partly caused by increased oxidative and nitrative stress. The majority of reactive oxygen and nitrogen spe...
The mechanism by which methanol causes blindness is as follows :- There is a enzyme (an alcohol dehydrogenase) in the eye which is responsible for turni...
Gene target information for ZADH2 - zinc binding alcohol dehydrogenase domain containing 2 (human). Find diseases associated with this biological target and compounds tested against it in bioassay experiments.
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Effect of Elaeagnus Conferta Roxb (Elaeagnaceae) Dry Fruit on the Activities of Hepatic Alcohol Dehydrogenase and Aldehyde Dehydrogenase in Mice. Chongming Wu; Rongji Dai; Jingmiao Bai; Yan Chen; Yuhong Yu; Weiwei Meng; Yulin Deng // Tropical Journal of Pharmaceutical Research;Dec2011, Vol. 10 Issue 6, p761 Purposes: To determine the effect of Elaeagnus conferta Roxb dry fruit powder (ECR) on blood alcohol clearance and on the activities of hepatic alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). Methods: In a randomized controlled study, acute alcohol intoxication was induced in mice... ...
A genomic DNA library of the bacterium Bacillus pumilus PLS was constructed and the beta-xylosidase gene (xynB) was amplified from a 3-kb genomic DNA fragment with the aid of the polymerase chain reaction technique. The amplified xynB gene was inserted between the yeast alcohol dehydrogenase II gene promoter (ADH2P) and terminator (ADH2T) sequences on a multicopy episomal plasmid (pDLG11). The xynB gene was also fused in-frame to the secretion signal sequence of the yeast mating pheromone a-factor (MFa1S) before insertion between the ADH2P and ADH2T sequences on a similar multicopy episomal plasmid (pDLG12). The resulting construct ADH2P-MFa1SxynB-ADH2T was designated XLO1. Both plasmids pDLG11 and pDLG12 were introduced into Saccharomyces cerevisiae but only the expression of the XLO1 gene yielded biologically functional beta-xylosidase. The total beta-xylosidase activity remained cell-associated with a maximum activity of 0.09 nkat/ml obtained when the recombinant S. cerevisiae strain was ...
Chronic alcohol consumption induces multi-organ damage, including alcoholic liver disease (ALD), pancreatitis and hypertension. Ethanol and ethanol metabolic products play a significant role in the manifestation of its toxicity. Ethanol metabolizes to acetaldehyde and produces reduced nicotinamide adenine dinucleotide (NADH) by cytosolic alcohol dehydrogenase. Ethanol metabolism mediated by cytochrome-P450 2E1 causes oxidative stress due to increased production of reactive oxygen species (ROS). Acetaldehyde, increased redox cellular state and ROS activate transcription factors, which in turn activate genes for lipid biosynthesis and offer protection of hepatocytes from alcohol toxicity. Sterol regulatory element binding proteins (SREBPs) and peroxisome proliferator activated-receptors (PPARs) are two key lipogenic transcription factors implicated in the development of fatty liver in alcoholic and non-alcoholic steatohepatitis. SREBP-1 is activated in the livers of chronic ethanol abusers. An increase in
Low concentrations of hexachlorophene (HCP) inhibit a number of pyridine nucleotide-linked dehydrogenase enzymes. The I₅₀ HCP concentrations were 105 μM for pig heart isocitrate dehydrogenase (ICD), 65 μM for horse liver alcohol dehydrogenase, 39 μM for torula yeast glucose-6-phosphate dehydrogenase (G6PD), 6.0 μM for beef heart malate dehydrogenase, and 1.6 μM for bovine liver glutamate dehydrogenase (GDH) at the enzyme concentrations tested. HCP exhibited cooperative inhibition of these enzymes since the observed maximum interaction coefficient, n, between HCP binding sites ranged between 1.62 and 3.33 but it was not an allosteric effector as evidenced by Hill coefficients for the substrates of approximately 1.0 both in the absence and the presence of HCP. More detailed kinetic analysis showed that HCP in most cases exhibited mixed kinetics, giving average K[subscript i] values with G6PD of 16.6 μM for NADP⁺ and 18.2 μM for glucose -6- phosphate; with ICD of 171 µM for NADP⁺ ...
302735543 - EP 0576621 B1 2001-02-28 - ETHANOL PRODUCTION BY RECOMBINANT HOSTS - [origin: WO9216615A1] Novel plasmids comprising genes which code for the alcohol dehydrogenase and pyruvate decarboxylase are described. Also described are recombinant hosts which have been transformed with genes coding for alcohol dehydrogenase and pyruvate. By virtue of their transformation with these genes, the recombinant hosts are capable of producing significant amounts of ethanol as a fermentation product. Also disclosed are methods for increasing the growth of recombinant hosts and methods for reducing the accumulation of undesirable metabolic products in the growth medium of these hosts. Also disclosed are recombinant host capable of producing significant amounts of ethanol as a fermentation product of oligosaccharides and plasmids comprising genes encoding polysaccharases, in addition to the genes described above which code for the alcohol dehydrogenase and pyruvate decarboxylase. Further, methods are described
1. The problem statement, all variables and given/known data Ethanol in the body is oxidized to acetaldehyde by liver alcohol dehydrogenase (LADH). Other...
Isozyme phenotypes of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) from human gastroendoscopic as well as surgical gastric biopsies were determined by starch gel electrophoresis and agarose isoelectric focusing. gamma gamma ADH isozy
3-AMINO-4-BROMO-2-METHYLPYRAZOLE 105675-85-2 NMR spectrum, 3-AMINO-4-BROMO-2-METHYLPYRAZOLE H-NMR spectral analysis, 3-AMINO-4-BROMO-2-METHYLPYRAZOLE C-NMR spectral analysis ect.
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The blood level of alcohol reflects the tissue levels throughout the body, and in a general way indicates the degree of impairment of the individual with drunke
Biocatalytic methods of synthesis are becoming increasingly important in industry. Using enzymes as catalysts allows highly selective reactions to be performed under milder physical conditions and in a more environmentally benign fashion than most corresponding chemical catalysts.. Enzymes have in general evolved to perform one type of reaction on a limited set of molecules, and hence there is often a need to alter the specificity of an enzyme to suit a desired process. Understanding the details of enzymatic catalysis at a quantum mechanical level enables the intelligent redesign of these macromolecules. For this purpose, density functional theory (DFT) has been shown to epitomise a suitable balance of accuracy and computational cost. Thus, this thesis describes the quantum chemical rationalisation of the reaction mechanism and sources of selectivity of the bacterial alcohol dehydrogenase TbSADH - an enzyme highly suited to modification for industrial processes.. ADHs catalyse reversibly the ...
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A disposable test strip device for detecting and measuring ethanol in aqueous solutions is disclosed. The test strip includes an inert support pad that contains a stabilized dry form of the enzyme alcohol oxidase, a material having peroxidative activity and an oxygen acceptor that reacts with hydrogen peroxide to give a compound of changed color. The use of this strip to determine ethanol levels colorimetrically is also disclosed.
He added that the implications of these findings go beyond significance for just researchers. "This is the sort of finding that reinforces the fact that genes impact on your response to alcohol, and impact on your risk for alcoholism," he said. "There are some people who think its hard to see behavioral problems like alcoholism being impacted by genes, but of course it is, because genes affect what you were like before you took the alcohol, and also genes absolutely impact on how the alcohol will affect you. The clearest example we have of this are the alcohol-metabolizing genes ...
Background Zinc is a component of various enzymes that help maintain structural integrity of proteins and regulate gene expression. Zinc metalloenzymes include ribonucleic acid polymerases, alcohol dehydrogenase, carbonic anhydrase and alkaline
In this work we characterize an alcohol dehydrogenase (ADH) from the hyperthermophilic archaeon Pyrobaculum aerophilum (PyAeADHII). We have previously found that PyAeADHII has no activity when standard ADH substrates are used but is active when α-tetralone is used as substrate. Here, to gain insights into enzyme function, we screened several chemical libraries for enzymatic modulators using an assay employing α-tetralone. The results indicate that PyAeADHII activity in the presence of α-tetralone was inhibited by compounds such as flunarizine. We also examined metal coordination of the enzyme in solution by performing metal substitution of the enzyme-bound zinc (Zn2+) with cobalt. The solution-based absorption spectra for cobalt substituted PyAeADHII supports substitution at the structural Zn2+ site. To gain structural insight, we obtained the crystal structure of both wild-type and cobalt-substituted PyAeADHII at 1.75 Å and 2.20 Å resolution, respectively. The X-ray data confirmed one ...
Lactic acid bacteria (LAB) are known for their high tolerance toward organic acids and alcohols (R. S. Gold, M. M. Meagher, R. Hutkins, and T. Conway, J. Ind. Microbiol. 10:45-54, 1992) and could potentially serve as platform organisms for production of these compounds. In this study, we attempted to redirect the metabolism of LAB model organism Lactococcus lactis toward ethanol production. Codon-optimized Zymomonas mobilis pyruvate decarboxylase (PDC) was introduced and expressed from synthetic promoters in different strain backgrounds. In the wild-type L. lactis strain MG1363 growing on glucose, only small amounts of ethanol were obtained after introducing PDC, probably due to a low native alcohol dehydrogenase activity. When the same strains were grown on maltose, ethanol was the major product and lesser amounts of lactate, formate, and acetate were formed. Inactivating the lactate dehydrogenase genes ldhX, ldhB, and ldh and introducing codon-optimized Z. mobilis alcohol dehydrogenase (ADHB) ...
A 3.2 kb fragment of an indigenous Anabaena azollae plasmid was isolated and fully sequenced. Sequence analysis identified an open reading frame of 1110-bp that showed high similarity (56-71%) with glutathione dependent formaldehyde dehydrogenase genes (gdfaldh) from various bacteria. The identity of the gene was confirmed by expressing the gene in Escherichia coli with a pET-32 (a) vector followed by enzyme assay. Adjacent to the gdfaldh a second gene was detected that showed high similarity (53%) with an S-formylglutathione hydrolase (fgh) gene from the methylotrophic bacterium Paracoccus denitrificans. The presence of gdfaldh and fgh-like genes adjacent to each other may suggest that the corresponding gene products interact in a common metabolic pathway involved in removing exogenous or endogenous formaldehyde ...
Looking for online definition of acyl-CoA dehydrogenase family member 9, mitochondrial in the Medical Dictionary? acyl-CoA dehydrogenase family member 9, mitochondrial explanation free. What is acyl-CoA dehydrogenase family member 9, mitochondrial? Meaning of acyl-CoA dehydrogenase family member 9, mitochondrial medical term. What does acyl-CoA dehydrogenase family member 9, mitochondrial mean?
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 ...
Dehydrogenase/reductase (SDR family) member 7 (DHRS7, retSDR4, SDR34C1) is a previously uncharacterized member of the short-chain dehydrogenase/reductase (SDR) superfamily. While human SDR members are known to play an important role in various (patho)biochemical pathways including intermediary metabolism and biotransformation of xenobiotics, only 20% of them are considered to be well characterized. Based on phylogenetic tree and SDR sequence clusters analysis DHRS7 is a close relative to well-known SDR member 11β-hydroxysteroid dehydrogenase 1 (11β-HSD1) that participates in metabolism of endogenous and xenobiotic substances with carbonyl group. The aim of present study is to determine the basic biochemical properties of DHRS7 and its possible involvement in metabolism of substrates with carbonyl group. For the first time the computational predictions of this membrane protein and membrane topology were experimentally confirmed. DHRS7 has been demonstrated to be an integral protein facing the lumen of
TY - JOUR. T1 - Levels of retinoic acid and retinaldehyde dehydrogenase expression in eyes of the Mitf-vit mouse model of retinal degeneration.. AU - Duncan, T.. AU - Swint, C.. AU - Smith, S. B.. AU - Wiggert, B. N.. PY - 1999/6/28. Y1 - 1999/6/28. N2 - PURPOSE: Several reports have characterized the retinal degeneration observed in the Mitf(vit) mutant mouse. Despite these reports, the factor(s) that may cause or modulate the degeneration still are not well defined; however, it is known that the photoreceptors of Mitf(vit) mice die through an apoptotic mechanism. We reported previously that retinoid metabolism in the RPE of Mitf(vit)++ mice is perturbed. Retinoids regulate genes via the RAR and RXR nuclear receptor pathway that are involved in numerous cellular responses including apoptosis. It is possible that retinoic acid (RA) modulates the retinal degeneration observed in the Mitf(vit) mice. The purpose of this study was to evaluate the levels of RA in whole eyes, as well as its ...

Thermoanaerobacter ethanolicus Wiegel and Ljungdahl ATCC ® 31550&tThermoanaerobacter ethanolicus Wiegel and Ljungdahl ATCC ® 31550&t

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 ...
more infohttps://atcc.org/en/Products/Cells_and_Microorganisms/Bacteria/Extremophiles/31550.aspx

Fetal alcohol spectrum disorder: Clinical features and diagnosisFetal alcohol spectrum disorder: Clinical features and diagnosis

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 ...
more infohttps://www.uptodate.com/contents/fetal-alcohol-spectrum-disorder-clinical-features-and-diagnosis

Mammalian alcohol dehydrogenase - Functional and structural implications | SpringerLinkMammalian alcohol dehydrogenase - Functional and structural implications | SpringerLink

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 ...
more infohttps://link.springer.com/article/10.1007/BF02255973

Alcohol dehydrogenase 1 - Catharanthus roseus (Madagascar periwinkle)Alcohol dehydrogenase 1 - Catharanthus roseus (Madagascar periwinkle)

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. * ...
more infohttps://www.uniprot.org/uniprot/P85440

Cross-reactive monoclonal antibodies to alcohol dehydrogenases | SpringerLinkCross-reactive monoclonal antibodies to alcohol dehydrogenases | SpringerLink

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- ...
more infohttps://link.springer.com/article/10.1007/BF01940438

alcohol dehydrogenase 7 Proteins: Novus Biologicalsalcohol dehydrogenase 7 Proteins: Novus Biologicals

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 ...
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alcohol dehydrogenase 5 Proteins: Novus Biologicalsalcohol dehydrogenase 5 Proteins: Novus Biologicals

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 ...
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Anti-Alcohol Dehydrogenase 2 Antibody Products | Biocompare.comAnti-Alcohol Dehydrogenase 2 Antibody Products | Biocompare.com

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 ...
more infohttps://www.biocompare.com/pfu/110447/soids/144790/Antibodies/Alcohol_Dehydrogenase_2

Alcohol dehydrogenase 1A - Saara hardwickii (Indian spiny-tailed lizard)Alcohol dehydrogenase 1A - Saara hardwickii (Indian spiny-tailed lizard)

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 ...
more infohttps://www.uniprot.org/uniprot/P25405

cinnamyl alcohol dehydrogenase
     Summary Report | CureHuntercinnamyl alcohol dehydrogenase Summary Report | CureHunter

cinnamyl alcohol dehydrogenase: NADP-dependent enzyme that catalyzes the reversible conversion of p-hydroxycinnamaldehydes to ... cinnamyl alcohol dehydrogenase. Subscribe to New Research on cinnamyl alcohol dehydrogenase NADP-dependent enzyme that ... 12/01/2014 - "Lignin and lignans in plant defence: insight from expression profiling of cinnamyl alcohol dehydrogenase genes ... "Molecular characterisation and expression of a wound-inducible cDNA encoding a novel cinnamyl-alcohol dehydrogenase enzyme in ...
more infohttp://www.curehunter.com/public/keywordSummaryC018656-cinnamyl-alcohol-dehydrogenase.do

Alcohol dehydrogenase - WikipediaAlcohol dehydrogenase - Wikipedia

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 ...
more infohttps://en.wikipedia.org/wiki/Alcohol_dehydrogenase

BRENDA - 1.1.1.90: aryl-alcohol dehydrogenaseBRENDA - 1.1.1.90: aryl-alcohol dehydrogenase

... alcohol dehydrogenase, arylalcohol dehydrogenase, BADH, benzyl alcohol dehydrogenase, CADH II, coniferyl alcohol dehydrogenase ... 1.1.1.90: aryl-alcohol dehydrogenase. This is an abbreviated version, for detailed information about aryl-alcohol dehydrogenase ... Application on EC 1.1.1.90 - 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, ...
more infohttp://www.brenda-enzymes.org/all_enzymes.php?ecno=1.1.1.90&table=Application

Alcohol dehydrogenase | definition of alcohol dehydrogenase by Medical dictionaryAlcohol dehydrogenase | definition of alcohol dehydrogenase by Medical dictionary

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: ...
more infohttp://medical-dictionary.thefreedictionary.com/alcohol+dehydrogenase

Anti-Alcohol Dehydrogenase antibody (HRP) - Azide free (ab34575) ReferencesAnti-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 ...
more infohttp://www.abcam.com/alcohol-dehydrogenase-antibody-hrp-azide-free-ab34575-references.html

Alcohol dehydrogenase class 4 mu/sigma chain - DrugBankAlcohol dehydrogenase class 4 mu/sigma chain - DrugBank

Alcohol dehydrogenase class 4 mu/sigma chain. Details. Name. Alcohol dehydrogenase class 4 mu/sigma chain. Kind. protein. ... Alcohol dehydrogenase class 4 mu/sigma chain. P40394. Details. Drug Relations. Drug Relations. DrugBank ID. Name. Drug group. ...
more infohttps://www.drugbank.ca/biodb/bio_entities/BE0000522

Alcohol dehydrogenase (quinone) - WikipediaAlcohol dehydrogenase (quinone) - Wikipedia

Alcohol dehydrogenase (quinone) (EC 1.1.5.5, type III ADH, membrane associated quinohaemoprotein alcohol dehydrogenase) is an ... "Quinoprotein alcohol dehydrogenase is involved in catabolic acetate production, while NAD-dependent alcohol dehydrogenase in ... "The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from ... Alcohol dehydrogenase (quinone) at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ...
more infohttps://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(quinone)

RCSB PDB 









- 1MGO: Horse Liver Alcohol Dehydrogenase Phe93Ala Mutant Literature Report PageRCSB PDB - 1MGO: Horse Liver Alcohol Dehydrogenase Phe93Ala Mutant Literature Report Page

Mobility of Fluorobenzyl Alcohols Bound to Liver Alcohol Dehydrogenases as Determined by NMR and X-ray Crystallographic Studies ... Alcohol Dehydrogenase E chain A, B 374 Equus caballus EC#: 1.1.1.1 IUBMB Mutation: F93A Gene Name(s): ... 2,3,4,5,6-PENTAFLUOROBENZYL ALCOHOL. C7 H3 F5 O PGJYYCIOYBZTPU-UHFFFAOYSA-N ...
more infohttp://www.rcsb.org/pdb/explore/litView.do?structureId=1MGO

Remediated Sequence 









- 1PED: BACTERIAL SECONDARY ALCOHOL DEHYDROGENASE (APO-FORM) Sequence Report PageRemediated Sequence - 1PED: BACTERIAL SECONDARY ALCOHOL DEHYDROGENASE (APO-FORM) Sequence Report Page

Crystalline alcohol dehydrogenases from the mesophilic bacterium Clostridium beijerinckii and the thermophilic bacterium ... Chain A: NADP-DEPENDENT ALCOHOL DEHYDROGENASE. Chain Downloadable Files. Download FASTA File. View Sequence & DSSP Image. ...
more infohttp://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1PED

4DXH: Horse Liver Alcohol Dehydrogenase Complexed With Nad+ And 2,2,2- Trifluoroethanol4DXH: Horse Liver Alcohol Dehydrogenase Complexed With Nad+ And 2,2,2- Trifluoroethanol

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. ...
more infohttps://www.ncbi.nlm.nih.gov/Structure/pdb/4DXH

Alcohol dehydrogenase molecule - Stock Image C035/5378 - Science Photo LibraryAlcohol dehydrogenase molecule - Stock Image C035/5378 - Science Photo Library

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 ...
more infohttp://www.sciencephoto.com/media/846461/view

Computational studies of human class V alcohol dehydrogenase - the odd siblingComputational 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 ...
more infohttp://www.diva-portal.org/smash/record.jsf?pid=diva2:1033016

Alcohol dehydrogenase, molecular model - Stock Image - A605/0212 - Science Photo LibraryAlcohol dehydrogenase, molecular model - Stock Image - A605/0212 - Science Photo Library

Alcohol dehydrogenase (ADH) is an enzyme that facilitates the break-down of alcohols in the body, which could otherwise be ... Alcohol dehydrogenase, molecular model. Alcohol dehydrogenase (ADH) is an enzyme that facilitates the break-down of alcohols in ... The alcohol is converted to acetaldehyde, an even more toxic molecule, which is then quickly converted into acetate and other ...
more infohttps://www.sciencephoto.com/media/6280/view/alcohol-dehydrogenase-molecular-model

WikiGenes - ADH1C - alcohol dehydrogenase 1C (class I), gamma...WikiGenes - ADH1C - alcohol dehydrogenase 1C (class I), gamma...

Avian alcohol dehydrogenase: the chicken liver enzyme. Primary structure, cDNA-cloning, and relationships to other alcohol ... Similarly, two different yeast glucose-6-phosphate dehydrogenases and a minor variant of a human alcohol dehydrogenase were ... Gene activation of alcohol dehydrogenase in Japanese quail and chicken-quail hybrid embryos. LeVine, J.P., Haley, L.E. Biochem ... Estrogen induction of alcohol dehydrogenase in the uropygial gland of mallard ducks. Hiremath, L.S., Kessler, P.M., Sasaki, G.C ...
more infohttps://www.wikigenes.org/e/gene/e/396299.html

WikiGenes - ADH4 - alcohol dehydrogenase 4 (class II), pi...WikiGenes - ADH4 - alcohol dehydrogenase 4 (class II), pi...

Synonyms: ADH-2, Alcohol dehydrogenase 4, Alcohol dehydrogenase class II pi chain, HEL-S-4 ... Baboon alcohol dehydrogenase isozymes: phenotypic changes in liver following chronic consumption of alcohol. Holmes, R.S., ... Association of alcohol dehydrogenase genes with alcohol dependence: a comprehensive analysis. Edenberg, H.J., Xuei, X., Chen, H ... Function of cis-acting elements in human alcohol dehydrogenase 4 (ADH4) promoter and role of C/EBP proteins in gene expression. ...
more infohttps://www.wikigenes.org/e/gene/e/127.html

Pharmaceutics | Free Full-Text | Encapsulation of Alcohol Dehydrogenase in Mannitol by  Spray DryingPharmaceutics | 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. ...
more infohttp://mdpi.com/1999-4923/6/1/185/xml
  • We offer alcohol dehydrogenase 7 Peptides and alcohol dehydrogenase 7 Proteins for use in common research applications: ELISA, Protein Array, Western Blot. (novusbio.com)
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  • Background: All known attempts to isolate and characterize mammalian class V alcohol dehydrogenase (class V ADH), a member of the large ADH protein family, at the protein level have failed. (diva-portal.org)
  • The SlscADH1 recombinant protein produced in Escherichia coli exhibited dehydrogenase-reductase activity towards several volatile compounds present in tomato flavour with a strong preference for the NAD/NADH co-factors. (nih.gov)
  • the role of decreased gastric alcohol dehydrogenase and first pass metabolism. (thefreedictionary.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)
  • Expression of alcohol dehydrogenase 3 (ADH3) in tissue and cultured cells from human oral mucosa. (springer.com)
  • In this work we characterize an alcohol dehydrogenase (ADH) from the hyperthermophilic archaeon Pyrobaculum aerophilum (PyAeADHII). (ku.edu)
  • Our alcohol dehydrogenase 7 Peptides and alcohol dehydrogenase 7 Proteins can be used in a variety of model species: Human. (novusbio.com)
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  • Cronholm T. Effect of ethanol on the redox state of the coenzyme bound to alcohol dehydrogenase studied in isolated hepatocytes. (springer.com)
  • A tomato short-chain dehydrogenase-reductase (SlscADH1) is preferentially expressed in fruit with a maximum expression at the breaker stage while expression in roots, stems, leaves and flowers is very weak. (nih.gov)
  • In U.hardwickii there are two isozymes of alcohol dehydrogenase I. (uniprot.org)