Kinetic mechanism of yeast alcohol dehydrogenase activity with secondary alcohols and ketones.
Indian J Biochem Biophys
;
1994 Oct; 31(5): 387-91
Article
in English
| IMSEAR
| ID: sea-28262
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.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Saccharomyces cerevisiae
/
Alcohol Dehydrogenase
/
Kinetics
/
Alcohols
/
Ketones
Language:
English
Journal:
Indian J Biochem Biophys
Year:
1994
Type:
Article
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