Regulation of two soluble forms of brain glutamate dehydrogenase isoproteins by protein kinases

Abstract

We isolated two soluble forms of glutamate dehydrogenase isoproteins, GDH I and GDH II, from bovine brain. The regulation of GDH I and GDH II by phosphorylation and dephosphorylation has been examined in various conditions. There were dose‐ and time‐ dependent activation of the GDH isoproteins when phosphorylated by cAMP‐dependent protein kinase. The phosphorylated GDH had 1.1 mol of covalently bound phosphate/mol of subunit and a 2‐fold increased specific activity. The phosphorylated amino acid was identified as serine. When treated with alkaline phosphatase, the activities of the phosphorylated GDH isoproteins were reduced in dose and time dependent manner and returned to those of unphosphorylated enzymes. There were no significant differences between GDH I and GDH II in their sensitivities to the action of phosphorylation and dephosphorylation, demonstrating that the microenvironmental structures of the phosphorylation site in GDH isoproteins are similar to each other. These results suggest that the in...