Kinetic mechanism of yeast alcohol dehydrogenase activity with secondary alcohols and ketones.
Indian J Biochem Biophys
; 1994 Oct; 31(5): 387-91
Article
Dans En
| 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.
Texte intégral:
1
Indice:
IMSEAR
Sujet Principal:
Saccharomyces cerevisiae
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Alcohol dehydrogenase
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Cinétique
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Alcools
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Cétones
langue:
En
Texte intégral:
Indian J Biochem Biophys
Année:
1994
Type:
Article