Kinetic mechanism of yeast alcohol dehydrogenase with primary aliphatic alcohols and aldehydes.
Yeast alcohol dehydrogenase (EC 1.1.1.1) catalyzes the interconversion of three redox pairs, ethanol/acetaldehyde, propanol/propionaldehyde and butanol/butyraldehyde by the same common mechanism, only with different magnitudes of rate constants. This general mechanism is Ordered Bi Bi in both directions, with the formation of abortive ternary complexes enzyme.NAD+.aldehyde and binary complexes enzyme.aldehyde.
Trivić
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Faculty of Sciences, Bulevar Cara Lazara, Novi Sad, Yogoslavia.
Leskovac
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D000426:Alcohol Dehydrogenase / Q000378:metabolism*; D000438:Alcohols / Q000378:metabolism*; D000447:Aldehydes / Q000378:metabolism*; D007700:Kinetics; D008433:Mathematics; D008962:Models, Theoretical; D009243:NAD / Q000378:metabolism; D011485:Protein Binding; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013379:Substrate Specificity
D000438:Alcohols; D000447:Aldehydes; D009243:NAD; D000426:Alcohol Dehydrogenase