Reactivation of the Phospho Form of the NAD‐Dependent Glutamate Dehydrogenase by a Yeast Protein Phosphatase
- 1 May 1981
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 116 (1) , 47-50
- https://doi.org/10.1111/j.1432-1033.1981.tb05298.x
Abstract
A protein phosphatase was isolated from the yeast, C. 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, NH4+ and NADH had no effect. The reactivation of phosphorylated glutamate dehydrogenase could be inhibited by phosphate, pyrophosphate and fluoride.This publication has 17 references indexed in Scilit:
- Phosphorylation-Dephosphorylation of EnzymesAnnual Review of Biochemistry, 1979
- The Regulation of Glutamate Metabolism in Candida utilisEuropean Journal of Biochemistry, 1977
- Purification and properties of a yeast protein kinaseBiochemistry, 1975
- Amino acid sequence of two functional sites in yeast glycogen phosphorylaseBiochemistry, 1975
- Functional similarity of yeast and mammalian adenosine 3′,5′-monophosphate-dependent protein kinasesBiochemical and Biophysical Research Communications, 1974
- Neurospora crassa pyruvate dehydrogenase: Interconversion by phosphorylation and dephosphorylationFEBS Letters, 1972
- Purification and properties of yeast glycogen phosphorylase a and bBiochemistry, 1971
- Interconvertible forms of glycogen synthetase in Neurospora crassaBiochimica et Biophysica Acta (BBA) - Enzymology, 1969
- Further Studies on the Site Phosphorylated in the Phosphorylase b to a Reaction*Biochemistry, 1964
- Determination of Inorganic PhosphateAnalytical Chemistry, 1949