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Title: Kinetic mechanism of yeast alcohol dehydrogenase activity with secondary alcohols and ketones. Author: Trivić S, Leskovac V. Journal: Indian J Biochem Biophys; 1994 Oct; 31(5):387-91. PubMed ID: 7851938. 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.[Abstract] [Full Text] [Related] [New Search]