期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1977
卷号：74
期号：8
页码：3239-3243
DOI：10.1073/pnas.74.8.3239
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The properties of purified mammalian adenosine 3':5'-cyclic monophosphate (cAMP)- and guanosine 3':5'-cyclic monophosphate (cGMP)-dependent protein kinases were compared. Several physical characteristics of the two enzymes were similar, including size, shape, affinity for cyclic nucleotide binding, and Km for ATP. In addition, the amino acid composition of the two proteins indicated a close composition homology (70-90%). Both cyclic nucleotide-dependent protein kinases catalyzed phosphorylation of rat liver pyruvate kinase (EC 2.7.1.40 ) and fructose 1,6-diphosphatase (EC 3.1.3.11 ), rabbit skeletal muscle glycogen synthase (EC 2.4.1.11 ) and phosphorylase b kinase (EC 2.7.1.38 ), and calf thymus histone H2b. The phosphorylation of several synthetic peptides and of trypsin-sensitive and trypsin-insensitive sites in glycogen synthase suggested similar recognition sites on the protein substrates for the two kinases. The cAMP-dependent protein kinase was the better catalyst with each protein or peptides substrate. The results suggest that the two enzymes evolved from a common ancestral protein.
