Use of pH studies to determine the kinetic and chemical mechanism of yeast alcohol dehydrogenase with primary aliphatic alcohols and aldehydes.

A complete list of all steady-state kinetic constants for the yeast alcohol dehydrogenase (EC 1.1.1.1) catalyzed oxidation of ethanol, propan-1-ol and butan-1-ol, and for the reduction of acetaldehyde and propionaldehyde was collected in the pH range 6-10, and an appropriate pH profile for each constant was constructed. A common minimal mechanism with all these substrates has been postulated and pKa values and the pH independent limiting values have been assigned for the rate constants.