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Literature summary extracted from

  • Wu, J.; Yang, J.; Kannan, N.; Madhusudan; Xuong, N.H.; Ten Eyck, L.F.; Taylor, S.S.
    Crystal structure of the E230Q mutant of cAMP-dependent protein kinase reveals an unexpected apoenzyme conformation and an extended N-terminal A helix (2005), Protein Sci., 14, 2871-2879.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.11.11 cAMP dependent on Mus musculus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.11.11 expression of catalytic subunit C mutant E230Q in Escherichia coli Mus musculus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.11.11 purified recombinant catalytic subunit C mutant E230Q in ternary complex with ATP, Mg2+, and IP20, hanging drop vapour diffusion method, protein solution versus reservoir solution containing 0.1 M bicine, pH 8.0, 13% 2-methyl-2,4-pentanediol, and 11% methanol, 4°C, cryoprotection by 15% glycerol, X-ray diffraction structure determination and analysis at 2.8 A resolution Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.11.11 E230Q site-directed mutagenesis, mutation of an acidic residue from the cluster around the active site of the catalytic subunit C, E230 forms the salt bridge required for interaction with the substrate, mutant shows decreased substrate recognition, phosphorylation degree, and activity compared to the wild-type subunit C, mutant has an open conformation and does not bind ligands like MgATP2- or IP20 inhibitor Mus musculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.11 IP20
-
 Mus musculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.11.11 Mg2+ the Mg-positioning loop consists of residues Asp184-Phe187 Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.11 Mus musculus P05132
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.11.11 phosphoprotein the enzyme can be phosphorylated at Thr197, Ser338, Ser10, and Ser139, the phosphorylation status of the enzyme varies, and is chronically reduced in enzyme mutant E230Q Mus musculus

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.11.11 recombinant catalytic subunit C mutant E230Q from Escherichia coli Mus musculus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.11.11 ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate substrate binding site structure involving E230, the electrostatic surface is important for substrate binding and catalysis, and also for the mechanism of closing the active site cleft of subunit C, conformation and mechanism, overview, the catalytic loop consists of residues Arg165-Asn171 Mus musculus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.11 ATP + a protein
-
 Mus musculus ADP + a phosphoprotein
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.11.11 PKA
-
 Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.11 ATP binding pocket and small lobe structure, binding involves D166, N171, D184, and K72 Mus musculus