EC - CGMP-dependent protein kinase

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IntEnz Enzyme Nomenclature


Accepted name:
cGMP-dependent protein kinase
Other names:
3':5'-cyclic GMP-dependent protein kinase
cGMP-dependent protein kinase Iβ
guanosine 3':5'-cyclic monophosphate-dependent protein kinase
PKG 1α
PKG 1β
Systematic name:
ATP:protein phosphotransferase (cGMP-dependent)



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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00100
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004692
UniProtKB/Swiss-Prot: (12) [show] [UniProt]


  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: 3918-3922 (1976). [PMID: 186778]
  2. Murthy, K.S.
    Modulation of soluble guanylate cyclase activity by phosphorylation.
    Neurochem. Int. 45: 845-851 (2004). [PMID: 15312978]
  3. Richie-Jannetta, R., Francis, S.H. and Corbin, J.D.
    Dimerization of cGMP-dependent protein kinase Ibeta is mediated by an extensive amino-terminal leucine zipper motif, and dimerization modulates enzyme function.
    J. Biol. Chem. 278: 50070-50079 (2003). [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: 31929-31936 (1997). [PMID: 9395542]

[EC created 2005 (EC part-incorporated 2005)]