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PMID: 198777 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Adenosine 3':5'-cyclic monophosphate- and guanosine 3':5'-cyclic monophosphate-dependent protein kinases: possible homologous proteins.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 74 ·No. 8 ·1977-08-00 ·Pages 3239-43

Lincoln TM, Corbin JD

Abstract

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 K(m) 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 H(2)b. 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.

MeSH Terms
Amino Acid Sequence Amino Acids/analysis Animals Cattle Cyclic AMP/pharmacology Cyclic GMP/pharmacology Enzyme Activation Kinetics Liver/enzymology Lung/enzymology Molecular Weight Myocardium/enzymology Peptide Fragments/analysis Protamine Kinase/metabolism Protein Kinases/metabolism Substrate Specificity
Chemicals
Amino Acids Peptide Fragments Cyclic AMP Protein Kinases Protamine Kinase Cyclic GMP
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Lincoln T M
Corbin J D
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36 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.74.8.3239
Published
1977-08-00
Pages
3239-43
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC431514
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.74.8.3239 PMC Full Text View journal details
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