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. 1979 Dec;140(3):874–880. doi: 10.1128/jb.140.3.874-880.1979

Regulation of activity and synthesis of N-acetylglutamate synthase from Saccharomyces cerevisiae.

B Wipe, T Leisinger
PMCID: PMC216728  PMID: 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.

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Selected References

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