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Literature summary for 2.7.11.11 extracted from

  • Ung, M.; Lu, B.; McCammon, J.A.
    E230Q mutation of the catalytic subunit of cAMP-dependent protein kinase affects local structure and the binding of peptide inhibitor (2006), Biopolymers, 81, 428-439.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallization of the muatnt E230Q with MgATP2- and protein kinase inhibitor is only possible as apoenzyme, analysis of the mechanism preventing ternary complex formation by relaxed-complex method Mus musculus

Protein Variants

Protein Variants Comment Organism
E230Q site-directed mutagenesis of the catalytic subunit, the mutation affects the local structure of the the F-to-G helix loop and asp241, and the binding of protein kinase inhibitor PKI, the mutant protein can only be crystallizes as apoenzyme Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
protein kinase inhibitor PKI binding structure, overview Mus musculus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus P05132
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + kemptide
-
Mus musculus ADP + phospho-kemptide
-
?
additional information the catalytic subunit has a cluster of nonconserved acidic residues, Glu127, Glu170, Glu203, Glu230, and Asp241, that are crucial for substrate recognition and binding Mus musculus ?
-
?

Subunits

Subunits Comment Organism
More the catalytic subunit has a cluster of nonconserved acidic residues, Glu127, Glu170, Glu203, Glu230, and Asp241, that are crucial for substrate recognition and binding, protein dynamics of the catalytic C-subunit, overview Mus musculus

Synonyms

Synonyms Comment Organism
PKA
-
Mus musculus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Mus musculus