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Literature summary for 2.7.11.17 extracted from

  • Robison, A.J.; Winder, D.G.; Colbran, R.J.; Bartlett, R.K.
    Oxidation of calmodulin alters activation and regulation of CaMKII (2007), Biochem. Biophys. Res. Commun., 356, 97-101.
    View publication on PubMedView publication on EuropePMC
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Activating Compound

Activating Compound Comment Organism Structure
Calmodulin dependent on, activating activity is abolished by calmodulin oxidation, phosphorylation of substrate by CaMKII and CaMKII autophosphorylation at Thr286, calmodulin binding to the enzyme inhibits autophosphorylation at Thr305/Thr306, which leads to enzyme inhibition, overview Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ dependent on, activates phosphorylation of substrate by CaMKII and CaMKII autophosphorylation at Thr286 Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein the enzyme performs autophosphorylation at Thr286, activating the enzyme, and at Thr305/Thr306 of the calmodulin binding site inhibiting the enzyme Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Rattus norvegicus
-
forebrain
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme performs autophosphorylation at Thr286 activating the enzyme activity, and at Thr305/Thr306, which inhibits calmodulin binding and enzyme activation Rattus norvegicus ?
-
 ?

Synonyms

Synonyms Comment Organism
CaMKII
-
 Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Rattus norvegicus