|Related Categories||1.1.x.x Acting on hydroxyl groups, 1.x.x.x Oxidoreductases, Alcohol Metabolism, Application Index, Biochemicals and Reagents,|
|contains||citrate as stabilizer|
|lactose as stabilizer|
One unit will convert 1.0 μmole of ethanol to acetaldehyde per min at pH 8.8 at 25 °C.
Alcohol dehydrogenase may be used to synthesize enantiomerically pure stereoisomers of chiral alcohols. It may be used to study ethanol fuel cells, alcoholism and drug dependence 1. Product A2529 is from S. Cerevisiae and is an insoluble enzyme with endless applications.
Sigma insoluble enzymes are produced by reacting a soluble enzyme with an inert base. This produces an insoluble compound with the activity of the original enzyme. Alcohol dehydrogenase has broad substrate specificity for alcohols, ketones and acetaldehyde.
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recombinant, expressed in E. coli, ≥10.0 U/mL
lyophilized powder (contains buffer salts), ≥300 units/mg protein
≥300 units/mg protein
1. OBJECTIVE The objective of this procedure is to standardize the enzymatic assay of Alcohol Dehydrogenase attached to Agarose, Sigma Product Number (A2529) , at Sigma-Aldrich St. Louis.
Keywords: Extinction coefficient
This procedure may be used for Alcohol Dehydrogenase products, except for Alcohol Dehydrogenase, Insoluble Enzyme attached to beaded agarose (Catalog No. A2529).
Keywords: Extinction coefficient
From our library of Related Content, Sigma-Aldrich presents Enzyme Explorer: the most comprehensive source of enzymes, substrates, activators, & inhibitors.
Keywords: Cell culture, Cell disruption, Cell signaling, Diagnostic, Digestions, Drug discovery, Functional genomics, Gene expression, Genomics, Metabolic Pathways, Molecular biology, Neuroscience, Proteomics
Alcohol dehydrogenase and aldehyde dehydrogenase gene polymorphisms, alcohol intake and the risk of colorectal cancer in the European Prospective Investigation into Cancer and Nutrition study. Ferrari P, McKay JD, Jenab M, et al. Eur. J. Clin. Nutr. 66(12), 1303-8, (2012)
Effects of the extracts and an active compound curcumenone isolated from Curcuma zedoaria rhizomes on alcohol-induced drunkenness in mice. Kimura Y, Sumiyoshi M, and Tamaki T Fitoterapia 84, 163-9, (2013)
Biocatalytic characterization of a short-chain alcohol dehydrogenase with broad substrate specificity from thermophilic Carboxydothermus hydrogenoformans. Zhou S, Zhang SC, Lai DY, et al. Biotechnol. Lett. 35(3), 359-65, (2013)
Metabolism and pharmacokinetics of 3-n-butylphthalide (NBP) in humans: the role of cytochrome P450s and alcohol dehydrogenase in biotransformation. Diao X, Deng P, Xie C, et al. Drug Metab. Dispos. 41(2), 430-44, (2013)
The bifunctional aldehyde-alcohol dehydrogenase controls ethanol and acetate production in Entamoeba histolytica under aerobic conditions. Pineda E, Encalada R, Olivos-García A, et al. FEBS Lett. 587(2), 178-84, (2013)
Expression pattern, ethanol-metabolizing activities, and cellular localization of alcohol and aldehyde dehydrogenases in human small intestine. Chiang CP, Wu CW, Lee SP, et al. Alcohol. Clin. Exp. Res. 36(12), 2047-58, (2012)
Hydrogen-driven asymmetric reduction of hydroxyacetone to (R)-1,2-propanediol by Ralstonia eutropha transformant expressing alcohol dehydrogenase from Kluyveromyces lactis. Oda T, Oda K, Yamamoto H, et al. Microb. Cell Fact. 12(1), 2, (2013)
Inhibition of CYP2E1 leads to decreased malondialdehyde-acetaldehyde adduct formation in VL-17A cells under chronic alcohol exposure. Swaminathan K, Clemens DL, and Dey A Life Sci. 92(6-7), 325-36, (2013)
[Effect of Cu2+ on synthesis of biosurfactants of Acinetobacter calcoaceticus IMV B-7241 and Rhodococcus erythropolis IMV Ac-5017]. Pirog TP, Konon AD, Sofilkanich AP, et al. Mikrobiol. Z. 75(1), 3-13, (2013)
The complete structure of human class IV alcohol dehydrogenase (retinol dehydrogenase) determined from the ADH7 gene. Satre MA, Zgombić-Knight M, and Duester G J. Biol. Chem. 269(22), 15606-12, (1994)
Structure of the class II enzyme of human liver alcohol dehydrogenase: combined cDNA and protein sequence determination of the pi subunit. Höög JO, von Bahr-Lindström H, Hedén LO, et al. Biochemistry 26(7), 1926-32, (1987)
Class IV alcohol dehydrogenase (the gastric enzyme). Structural analysis of human sigma sigma-ADH reveals class IV to be variable and confirms the presence of a fifth mammalian alcohol dehydrogenase class. Parés X, Cederlund E, Moreno A, et al. FEBS Lett. 303(1), 69-72, (1992)
Expression and kinetic characterization of recombinant human stomach alcohol dehydrogenase. Active-site amino acid sequence explains substrate specificity compared with liver isozymes. Kedishvili NY, Bosron WF, Stone CL, et al. J. Biol. Chem. 270(8), 3625-30, (1995)
Genomic structure and expression of the ADH7 gene encoding human class IV alcohol dehydrogenase, the form most efficient for retinol metabolism in vitro. Zgombić-Knight M, Foglio MH, and Duester G J. Biol. Chem. 270(9), 4305-11, (1995)
The gamma 1 and gamma 2 subunits of human liver alcohol dehydrogenase. cDNA structures, two amino acid replacements, and compatibility with changes in the enzymatic properties. Höög JO, Hedén LO, Larsson K, et al. Eur. J. Biochem. 159(2), 215-8, (1986)
Class III human liver alcohol dehydrogenase: a novel structural type equidistantly related to the class I and class II enzymes. Kaiser R, Holmquist B, Hempel J, et al. Biochemistry 27(4), 1132-40, (1988)
Mutation of Arg-115 of human class III alcohol dehydrogenase: a binding site required for formaldehyde dehydrogenase activity and fatty acid activation. Engeland K, Höög JO, Holmquist B, et al. Proc. Natl. Acad. Sci. U. S. A. 90(6), 2491-4, (1993)
Role of arginine 115 in fatty acid activation and formaldehyde dehydrogenase activity of human class III alcohol dehydrogenase. Holmquist B, Moulis JM, Engeland K, et al. Biochemistry 32(19), 5139-44, (1993)
Alcohol dehydrogenase of class IV (sigma sigma-ADH) from human stomach. cDNA sequence and structure/function relationships. Farrés J, Moreno A, Crosas B, et al. Eur. J. Biochem. 224(2), 549-57, (1994)
Genetic polymorphism of alcohol dehydrogenase in europeans: the ADH2*2 allele decreases the risk for alcoholism and is associated with ADH3*1. Borràs E, Coutelle C, Rosell A, et al. Hepatology 31(4), 984-9, (2000)
Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions. Hurley TD, Bosron WF, Hamilton JA, et al. Proc. Natl. Acad. Sci. U. S. A. 88(18), 8149-53, (1991)
Molecular analysis of the human class I alcohol dehydrogenase gene family and nucleotide sequence of the gene encoding the beta subunit. Duester G, Smith M, Bilanchone V, et al. J. Biol. Chem. 261(5), 2027-33, (1986)
The human beta 3 alcohol dehydrogenase subunit differs from beta 1 by a Cys for Arg-369 substitution which decreases NAD(H) binding. Burnell JC, Carr LG, Dwulet FE, et al. Biochem. Biophys. Res. Commun. 146(3), 1127-33, (1987)
Human liver alcohol dehydrogenase: amino acid substitution in the beta 2 beta 2 Oriental isozyme explains functional properties, establishes an active site structure, and parallels mutational exchanges in the yeast enzyme. Jörnvall H, Hempel J, Vallee BL, et al. Proc. Natl. Acad. Sci. U. S. A. 81(10), 3024-8, (1984)
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