Regulation of activity and synthesis of N-acetylglutamate synthase from Saccharomyces cerevisiae.
J Bacteriol
; 140(3): 874-80, 1979 Dec.
Article
en En
| MEDLINE
| ID: mdl-391804
ABSTRACT
Feedback inhibition of N-acetylgutamate synthase in a particulate fraction from Saccharomyces cerevisiae by L-arginine was synergistically enhanced by N-actylglutamate, whereas coenzyme A let to an additive enhancement of arginine inhibition. N-acetylglutamate synthase was not inhibited by polyamines, nor was the enzyme inactivated by incubation in the presence of coenzyme A and zinc ions. Evidence was obtained for the involvement of at least three different regulatory mechanisms in the expression of N-acetylglutamate synthase arginine-specific repression, glucose repression and general amino acid control. The combined action of these control mechanisms led to a 90-fold variation in the specific activity of the enzyme.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Saccharomyces cerevisiae
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Acetiltransferasas
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Coenzima A
Idioma:
En
Año:
1979
Tipo del documento:
Article