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Literature summary extracted from

  • Byeon, I.J.; Dao, K.K.; Jung, J.; Keen, J.; Leiros, I.; Doskeland, S.O.; Martinez, A.; Gronenborn, A.M.
    Allosteric communication between cAMP binding sites in the RI subunit of protein kinase A revealed by NMR (2010), J. Biol. Chem., 285, 14062-14070.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.11.11 cAMP activation of protein kinase A involves the synergistic binding of cAMP to two cAMP binding sites on the inhibitory R subunit, causing release of the C subunit, which subsequently can carry out catalysis Bos taurus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.11.11 additional information generation of a construct RIalpha-(98-381) subunit comprising both cyclic nucleotide binding domains, in the presence and absence of cAMP, mapping the effects of cAMP binding at single residue resolution, NMR study, overview Bos taurus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.11.11 Mg2+ required Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.11 Bos taurus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.11 ATP + Leu-Arg-Arg-Ala-Ser-Leu-Gly commercial artificial heptapeptide substrate kemptide Bos taurus ADP + Leu-Arg-Arg-Ala-phospho-Ser-Leu-Gly
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.11.11 PKA
-
 Bos taurus
2.7.11.11 protein kinase A
-
 Bos taurus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.11.11 25
-
 assay at Bos taurus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.11.11 7.2
-
 assay at Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.11 ATP
-
 Bos taurus

General Information

EC Number General Information Comment Organism
2.7.11.11 additional information several conformationally disordered regions in free RIalpha become structured upon cAMP binding, including the interdomain alphaC:A and alphaC':A helices that connect cyclic nucleotide binding domains A and B and are primary recognition sites for the C subunit, unidirectional allosteric communication between the sites, Trp262, which lines the cyclic nucleotide binding A site but resides in the sequence of domain B, is an important structural determinant for intersite communication, overview Bos taurus