The Enzyme Database

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EC 2.7.11.11     
Accepted name: cAMP-dependent protein kinase
Reaction: ATP + a protein = ADP + a phosphoprotein
Other name(s): PKA; PKA C; protein kinase A; STK22
Systematic name: ATP:protein phosphotransferase (cAMP-dependent)
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].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 142008-29-5
References:
1.  Technikova-Dobrova, Z., Sardanelli, A.M., Speranza, F., Scacco, S., Signorile, A., Lorusso, V. and Papa, S. Cyclic adenosine monophosphate-dependent phosphorylation of mammalian mitochondrial proteins: enzyme and substrate characterization and functional role. Biochemistry 40 (2001) 13941–13947. [PMID: 11705384]
2.  Andersen, M.D., Shaffer, J., Jennings, P.A. and Adams, J.A. 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 (2001) 14204. [PMID: 11278927]
3.  Johnson, K.E., Cameron, S., Toda, T., Wigler, M. and Zoller, M.J. 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 (1987) 8636–8642. [PMID: 3036817]
4.  Haq, E., Sharma, S. and Khuller, G.K. Purification and characterization of cAMP dependent protein kinase from Microsporum gypseum. Biochim. Biophys. Acta 1474 (2000) 100–106. [PMID: 10699496]
[EC 2.7.11.11 created 2005 (EC 2.7.1.37 part-incorporated 2005)]
 
 


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