title: Carboxymethylated liver alcohol dehydrogenase: pH dependence of hydride transfer during ethanol oxidation.
abstract: The rate constant for the hydride transfer step during oxidation of ethanol by carboxymethylated alcohol dehydrogenase (alcohol: NAD+ oxidoreductase, EC 1.1.1.1) is dependent on a group with pKa 7.5. This pKa is higher than that for the native enzyme. A mechanism is proposed to account for the ionisation and the protein fluorescence change which occur during formation of the carboxymethylated enzyme-NAD+-ethanol complex.
authors.forename: M J
authors.initials: MJ
authors.lastname: Hardman
authors.forename: P H
authors.initials: PH
authors.lastname: Mills
mesh_terms: D000426:Alcohol Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000818:Animals; D000431:Ethanol / Q000378:metabolism*; D006736:Horses; D006863:Hydrogen-Ion Concentration; D007461:Iodoacetates / Q000494:pharmacology*; D019807:Iodoacetic Acid; D007700:Kinetics; D008099:Liver / Q000201:enzymology*
chemical_list: D007461:Iodoacetates; D000431:Ethanol; D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase; D019807:Iodoacetic Acid