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Literature summary for 2.7.11.11 extracted from

  • Cheng, Y.; Zhang, Y.; McCammon, J.A.
    How does activation loop phosphorylation modulate catalytic activity in the cAMP-dependent protein kinase: a theoretical study (2006), Protein Sci., 15, 672-683.
    View publication on PubMedView publication on EuropePMC
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Activating Compound

Activating Compound Comment Organism Structure
additional information activation loop phosphorylation at Thr197 regulates the enzyme's catalytic activity, molecular mechanism, classical molecular dynamics simulations and ab initio QM/MM calculations are carried out on the wild-type PKA-Mg2+- ATP-substrate complex and its dephosphorylated mutant, T197A, overview Homo sapiens

Protein Variants

Protein Variants Comment Organism
R165A site-directed mutagenesis, the mutant cannot be phosphorylated at Thr197 of the activation loop, molecular dynamics simulations, overview Homo sapiens
T197A site-directed mutagenesis, the side-chain conformations of the P-site Ser in the R165A mutant are similar to that in the wild-type PKA, although the replacement of Arg165 with Ala disconnects the interactions between the pThr 197 and the active site, molecular dynamics simulations, overview Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ PKA-Mg2+-ATP-substrate complex formation and effects on enzyme activity and stability, overview Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein activation loop phosphorylation at Thr197 regulates the enzyme's catalytic activity, molecular mechanism, classical molecular dynamics simulations and ab initio QM/MM calculations are carried out on the wild-type PKA-Mg2+- ATP-substrate complex and its dephosphorylated mutant, T197A, overview Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information phosphorylated residue pThr197 not only facilitates the phosphoryl transfer reaction by stabilizing the transition state through electrostatic interactions but also strongly affects its essential protein dynamics as well as the active site conformation, overview, free energy difference is,1.4 kcal/mol, it is necessary that Asp166 is available as the catalytic base to accept the hydroxyl proton in the late stages of the phosphoryl transfer Homo sapiens ?
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 ?

Subunits

Subunits Comment Organism
More structure of the ternary PKA-substrate complex, overview Homo sapiens

Synonyms

Synonyms Comment Organism
PKA
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP PKA-Mg2+-ATP-substrate complex formation and effects on enzyme activity and stability, overview Homo sapiens