V. Leskovac et al., USE OF PH STUDIES TO DETERMINE THE KINETIC AND CHEMICAL MECHANISM OF YEAST ALCOHOL-DEHYDROGENASE WITH PRIMARY ALIPHATIC-ALCOHOLS AND ALDEHYDES, Indian Journal of Biochemistry & Biophysics, 33(3), 1996, pp. 177-183
A complete list of all steady-state:kinetic constants for the yeast al
cohol dehydrogenase (EC 1.1.1.1) catalyzed oxidation of ethanol, propa
n-1-ol and butan-1-ol, and for the reduction of acetaldehyde and propi
onaldehyde was collected in the pH range 6-10, and an appropriate pH p
rofile for each constant was constructed, A common minimal mechanism w
ith all these substrates has been postulated and pK(a) values and the
pH independent limiting values have been assigned for the rate constan
ts.