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Literature summary for 2.7.11.12 extracted from

  • Heil, W.G.; Landgraf, W.; Hofmann, F.
    A catalytically active fragment of cGMP-dependent protein kinase. Occupation of its cGMP-binding sites does not affect its phosphotransferase activity (1987), Eur. J. Biochem., 168, 117-121.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information aminoterminal dimerization site of cGMP-dependent protein kinase and the autophosphorylation site, present in this part, control not only the activation of the enzyme but also the cooperative binding characteristics of the intact enzyme Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus P00516
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-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein autophosphorylation Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + protein autophosphorylation Bos taurus ADP + phosphoprotein
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?

Synonyms

Synonyms Comment Organism
cGMP-dependent protein kinase 1, alpha isozyme
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Bos taurus

Cofactor

Cofactor Comment Organism Structure
cGMP dependent on Bos taurus