An Adenosine 3′,5′-Monophosphate-dependent Protein Kinase from Escherichia coli

Abstract

Abstract An enzyme present in Escherichia coli which catalyzes the phosphorylation of histone by ATP has been found to be stimulated by adenosine 3',5'-monophosphate (cyclic AMP). The rate of the enzyme-catalyzed phosphorylation of histone was increased by about 300% at concentrations of cyclic AMP above 7 x 10-7 m. The apparent Km of the E. coli enzyme for cyclic AMP was about 2 x 10-7 m.