KINETIC MECHANISM OF YEAST ALCOHOL-DEHYDROGENASE ACTIVITY WITH SECONDARY ALCOHOLS AND KETONES

The kinetic mechanism of yeast alcohol dehydrogenase (EC 1.1.1.1) acti vity with the redox pair Z-propanol/acetone has been probed in detail by the application of initial rate studies in the absence and in the p resence of products, and a dead-end inhibitor pyrazole. An overall ste ady-state random Bi Bi mechanism in both directions, with the formatio n of both abortive ternary complexes, enzyme NADH.2-propanol and enzym e NAD(+).acetone has been observed. A complete list of steady-state ki netic constants are also reported for the redox pair (S)-(+)-2-butanol /2-butanone.