Wipe B, Leisinger T
J Bacteriol. 1979 Dec;140(3):874-80. doi: 10.1128/jb.140.3.874-880.1979.
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.
酿酒酵母颗粒组分中，L-精氨酸对N-乙酰谷氨酸合酶的反馈抑制作用被N-乙酰谷氨酸协同增强，而辅酶A则使精氨酸抑制作用呈加性增强。多胺不会抑制N-乙酰谷氨酸合酶，在辅酶A和锌离子存在的情况下孵育也不会使该酶失活。有证据表明，N-乙酰谷氨酸合酶的表达至少涉及三种不同的调节机制：精氨酸特异性阻遏、葡萄糖阻遏和一般氨基酸调控。这些调控机制的共同作用导致该酶的比活性有90倍的差异。
