Hemmings B A
Eur J Biochem. 1981 May;116(1):47-50. doi: 10.1111/j.1432-1033.1981.tb05298.x.
A protein phosphatase was isolated from the yeast, Candida utilis, which could reactivate (dephosphorylate) the phosphorylated form of the NAD-dependent glutamate dehydrogenase. The protein could also dephosphorylate casein, histone and kemptide (a heptapeptide corresponding to the phosphorylation site of liver pyruvate kinase). Reactivation of the phosphorylated glutamate dehydrogenase was stimulated by the simultaneous addition of NAD and L-glutamate; 2-oxoglutarate, NH+4 and NADH had no effect. The reactivation of phosphorylated glutamate dehydrogenase could be inhibited by phosphate, pyrophosphate and fluoride.
从产朊假丝酵母中分离出一种蛋白磷酸酶，它能使NAD依赖型谷氨酸脱氢酶的磷酸化形式重新激活（去磷酸化）。该蛋白也能使酪蛋白、组蛋白和肯普肽（一种与肝丙酮酸激酶磷酸化位点对应的七肽）去磷酸化。同时添加NAD和L-谷氨酸可刺激磷酸化谷氨酸脱氢酶的重新激活；2-氧代戊二酸、NH₄⁺和NADH则无作用。磷酸、焦磷酸和氟化物可抑制磷酸化谷氨酸脱氢酶的重新激活。
