EC 2 - Transferases
EC 2.7 - Transferring phosphorus-containing groups
EC 2.7.11 - Protein-serine/threonine kinases
EC 2.7.11.11 - CAMP-dependent protein kinase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 2.7.11.11
Names
Accepted name:
cAMP-dependent protein kinase
Other
names:
PKA
PKA C
protein kinase A
STK22
PKA C
protein kinase A
STK22
Systematic name:
ATP:protein phosphotransferase (cAMP-dependent)
Reaction
- ATP + a protein = ADP + a phosphoprotein
Comments:
cAMP is required to activate this enzyme. The inactive holoenzyme of cAMP-dependent protein kinase is a tetramer composed of two regulatory (R) and two catalytic (C) subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP molecules and two free monomeric catalytic subunits [i.e. R2C2 + 4 cAMP = R2(cAMP)4 + 2 C]. Formerly EC 2.7.1.37.
Links to other databases
Protein domains and families:
PROSITE:PDOC00100
Gene Ontology:
GO:0004679
,
GO:0004691
References
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Cyclic adenosine monophosphate-dependent phosphorylation of mammalian mitochondrial proteins: enzyme and substrate characterization and functional role.Biochemistry 40 : 13941-13947 (2001). [PMID: 11705384]
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Structural characterization of protein kinase A as a function of nucleotide binding. Hydrogen-deuterium exchange studies using matrix-assisted laser desorption ionization-time of flight mass spectrometry detection.J. Biol. Chem. 276 : 14204-14211 (2001). [PMID: 11278927]
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Expression in Escherichia coli of BCY1, the regulatory subunit of cyclic AMP-dependent protein kinase from Saccharomyces cerevisiae. Purification and characterization.J. Biol. Chem. 262 : 8636-8642 (1987). [PMID: 3036817]
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Purification and characterization of cAMP dependent protein kinase from Microsporum gypseum.Biochim. Biophys. Acta 1474 : 100-106 (2000). [PMID: 10699496]
[EC 2.7.11.11 created 2005 (EC 2.7.1.37 part-incorporated 2005)]