Activation enthalpies and pH dependence of phenol hydroxylase from Trichosporon cutaneum, in vitro and in situ.
FEBS Lett
; 242(1): 75-8, 1988 Dec 19.
Article
en En
| MEDLINE
| ID: mdl-3203745
ABSTRACT
The effect of pH and temperature on phenol hydroxylase in vitro was compared to the corresponding effect on the enzyme in situ, in permeabilized cells. Activation enthalpies in situ were about 75-80% of those in vitro, in both cases decreasing with increasing pH (6.0-8.5). The order of addition of phenol and NADPH affected the Km values for phenol at 25 degrees C, but not at 10 degrees C. The results support the idea that the enzyme in situ is in a more favourable position for catalysis than the purified enzyme and that slow conformational changes, triggered by binding of phenol, become rate limiting above 10 degrees C.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Trichosporon
/
Hongos Mitospóricos
/
Oxigenasas de Función Mixta
Idioma:
En
Revista:
FEBS Lett
Año:
1988
Tipo del documento:
Article
País de afiliación:
Suecia