Open AccessReactivation of the Phospho Form of the NAD‐Dependent Glutamate Dehydrogenase by a Yeast Protein Phosphatase
Author(s) -
HEMMINGS Brian A.
Publication year - 1981
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1981.tb05298.x
Subject(s) - glutamate dehydrogenase , nad+ kinase , biochemistry , dehydrogenase , phosphatase , phosphorylation , chemistry , glutamate receptor , biology , enzyme , receptor
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.