The Enzyme Database

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Accepted name: cGMP-dependent protein kinase
Reaction: ATP + a protein = ADP + a phosphoprotein
Other name(s): 3′:5′-cyclic GMP-dependent protein kinase; cGMP-dependent protein kinase Iβ; guanosine 3′:5′-cyclic monophosphate-dependent protein kinase; PKG; PKG 1α; PKG 1β; PKG II; STK23
Systematic name: ATP:protein phosphotransferase (cGMP-dependent)
Comments: CGMP is required to activate this enzyme. The enzyme occurs as a dimer in higher eukaryotes. The C-terminal region of each polypeptide chain contains the catalytic domain that includes the ATP and protein substrate binding sites. This domain catalyses the phosphorylation by ATP to specific serine or threonine residues in protein substrates [3]. The enzyme also has two allosteric cGMP-binding sites (sites A and B). Binding of cGMP causes a conformational change that is associated with activation of the kinase [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 141588-27-4
1.  Gill, G.N., Holdy, K.E., Walton, G.M. and Kanstein, C.B. Purification and characterization of 3′:5′-cyclic GMP-dependent protein kinase. Proc. Natl. Acad. Sci. USA 73 (1976) 3918–3922. [DOI] [PMID: 186778]
2.  Murthy, K.S. Modulation of soluble guanylate cyclase activity by phosphorylation. Neurochem. Int. 45 (2004) 845–851. [DOI] [PMID: 15312978]
3.  Richie-Jannetta, R., Francis, S.H. and Corbin, J.D. Dimerization of cGMP-dependent protein kinase Iβ is mediated by an extensive amino-terminal leucine zipper motif, and dimerization modulates enzyme function. J. Biol. Chem. 278 (2003) 50070–50079. [DOI] [PMID: 12933804]
4.  Zhao, J., Trewhella, J., Corbin, J., Francis, S., Mitchell, R., Brushia, R. and Walsh, D. Progressive cyclic nucleotide-induced conformational changes in the cGMP-dependent protein kinase studied by small angle X-ray scattering in solution. J. Biol. Chem. 272 (1997) 31929–31936. [DOI] [PMID: 9395542]
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