The activity of yeast ADH I and ADH II with long-chain alcohols and diols.
The activities of yeast ADH I and ADH II towards long chain alcohols and diols were studied using rather unusual conditions (1.0 M Tris pH 8.75, approximately 0.3 mg/ml enzyme and [S]<<<K(m) ) where the alcohols are oxidised quantitatively in a first-order manner. Plots of the apparent first-order rate constant versus primary alcohol chain length show double peaks with similar values for ethanol and 1-decanol and relatively low values for 1-butanol through to 1-octanol. With the alpha,omega diols only one peak of activity was observed with 1,14-tetradecanediol, the preferred substrate, being oxidised about the same rate as ethanol. Both enzymes were essentially inactive with short-chain diols (C(2)-C(8)). For all of these assays normalised rates with ADH II were about threefold faster than with ADH I.
Dickinson
F M
FM
Department of Biological Sciences, University of Hull, Cottingham Road, HU6 7RX, Hull, UK. f.m.dickinson@biosci.hull.ac.uk
Dack
S
S
D000426:Alcohol Dehydrogenase / Q000378:metabolism*; D000438:Alcohols / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D006736:Horses; D066298:In Vitro Techniques; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D010084:Oxidation-Reduction; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013379:Substrate Specificity
D000438:Alcohols; D000426:Alcohol Dehydrogenase