Kinetic mechanism of yeast alcohol dehydrogenase activity with secondary alcohols and ketones.
The kinetic mechanism of yeast alcohol dehydrogenase (EC 1.1.1.1) activity with the redox pair 2-propanol/acetone has been probed in detail by the application of initial rate studies in the absence and in the presence of products, and a dead-end inhibitor pyrazole. An overall steady-state random Bi Bi mechanism in both directions, with the formation of both abortive ternary complexes, enzyme.NADH.2-propanol and enzyme.NAD+.acetone has been observed. A complete list of steady-state kinetic constants are also reported for the redox pair (S)-(+)-2-butanol/2-butanone.
Trivić
S
S
Faculty of Sciences, Novi Sad, Yugoslavia.
Leskovac
V
V
D000426:Alcohol Dehydrogenase / Q000378:metabolism*; D000438:Alcohols / Q000378:metabolism*; D007659:Ketones / Q000378:metabolism*; D007700:Kinetics; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D000438:Alcohols; D007659:Ketones; D000426:Alcohol Dehydrogenase