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1.
Indian J Biochem Biophys ; 1996 Jun; 33(3): 177-83
Artículo en Inglés | IMSEAR | ID: sea-27608

RESUMEN

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.


Asunto(s)
Alcohol Deshidrogenasa/química , Alcoholes/química , Aldehídos/química , Concentración de Iones de Hidrógeno , Cinética , Modelos Químicos , Saccharomyces cerevisiae/enzimología , Especificidad por Sustrato
2.
Indian J Biochem Biophys ; 1994 Oct; 31(5): 387-91
Artículo en Inglés | IMSEAR | ID: sea-28262

RESUMEN

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.


Asunto(s)
Alcohol Deshidrogenasa/metabolismo , Alcoholes/metabolismo , Cetonas/metabolismo , Cinética , Saccharomyces cerevisiae/enzimología
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