Kinetic mechanism of yeast alcohol dehydrogenase activity with secondary alcohols and ketones.

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1994-10-01
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Abstract
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.
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Trivić S, Leskovac V. Kinetic mechanism of yeast alcohol dehydrogenase activity with secondary alcohols and ketones. Indian Journal of Biochemistry & Biophysics. 1994 Oct; 31(5): 387-91
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https://imsear.searo.who.int/handle/123456789/28262
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Indian Journal of Biochemistry & Biophysics