Abdelal A T, Nainan O V
J Bacteriol. 1979 Feb;137(2):1040-2. doi: 10.1128/jb.137.2.1040-1042.1979.
N-Acetylglutamate synthase was purified to homogeneity from Salmonella typhimurium. The enzyme is subject to repression and feedback inhibition by arginine. Inhibition studies indicated that arginine exerts its effect primarily by reducing the affinity of the enzyme for glutamate.
从鼠伤寒沙门氏菌中纯化出了N-乙酰谷氨酸合酶,且该酶已达到同质状态。该酶受到精氨酸的阻遏和反馈抑制。抑制研究表明,精氨酸主要通过降低该酶对谷氨酸的亲和力来发挥其作用。