Pyridine nucleotide-linked oxidation of methanol in methanol-assimilating yeasts.
An alcohol dehydrogenase linked to nicotinamide adenine dinucleotide and requiring glutathione has been isolated and partially purified from two methanol-assimilating yeasts. It differs from previously described methanol-oxidizing enzymes in pH optima, electron acceptor specificity, substrate specificity, inhibition pattern, and stability.
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D001203:Ascomycota / Q000378:metabolism*; D002175:Candida / Q000201:enzymology / Q000378:metabolism*; D002474:Cell-Free System; D002729:Chloromercuribenzoates / Q000494:pharmacology; D004355:Drug Stability; D005978:Glutathione / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007460:Iodoacetamide / Q000494:pharmacology; D008670:Metals / Q000494:pharmacology; D000432:Methanol / Q000378:metabolism*; D009243:NAD / Q000378:metabolism; D010084:Oxidation-Reduction; D010843:Pichia / Q000201:enzymology / Q000378:metabolism*; D013045:Species Specificity
D002729:Chloromercuribenzoates; D008670:Metals; D009243:NAD; D000429:Alcohol Oxidoreductases; D005978:Glutathione; D000432:Methanol; D007460:Iodoacetamide