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Literature summary for 2.7.11.11 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

Activating Compound Comment Organism Structure
cAMP dependent on Mus musculus

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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

Inhibitors Comment Organism Structure
IP20
-
Mus musculus

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Mus musculus P05132
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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)

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

Reaction

Reaction Comment Organism Reaction ID
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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
PKA
-
Mus musculus

Cofactor

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