Cofactor requirements of steroid-17-20-desmolase and 20 alpha-hydroxysteroid dehydrogenase activities in cell extracts of Clostridium scindens.
J Steroid Biochem
; 28(1): 49-54, 1987 Jul.
Article
en En
| MEDLINE
| ID: mdl-3475510
ABSTRACT
Two neutral steroid-transforming activities were demonstrated in cell extracts of Clostridium scindens. Steroid-17-20-desmolase and 20 alpha-hydroxysteroid dehydrogenase were found to be inducible in cells cultured in the presence of cortisol. Both activities required manganese ions and NAD+ or NADH for activity. Cortisol, cortisone and 11-desoxycortisol were substrates as well as inducers of steroid-17-20-desmolase and 20 alpha-hydroxysteroid dehydrogenase activities. 17 alpha-Hydroxyprogesterone was an effective inducer but did not serve as a substrate for either enzyme activity. C. scindens is the first bacterial species of the normal human intestinal flora reported to elaborate inducible steroid-17-20-desmolase and 20 alpha-hydroxysteroid dehydrogenase activities. The results of cofactor, substrate specificity and induction studies suggest that these two activities may reside in the same enzyme complex.
Buscar en Google
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Clostridium
/
Sistema Enzimático del Citocromo P-450
/
Aldehído-Liasas
/
20-Hidroxiesteroide Deshidrogenasas
Idioma:
En
Revista:
J Steroid Biochem
Año:
1987
Tipo del documento:
Article