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Literature summary extracted from

  • Loog, M.; Oskolkov, N.; O'Farrell, F.; Ek, P.; Järv, J.
    Comparison of cAMP-dependent protein kinase substrate specificity in reaction with proteins and synthetic peptides (2005), Biochim. Biophys. Acta, 1747, 261-266.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.11.11 cAMP dependent on Zea mays

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.11.11 0.021
-
RRASVA pH 7.5, 25°C, catalytic subunit Zea mays

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.11.11 Mg2+
-
Zea mays

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.11 Zea mays
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.11 ATP + L-pyruvate kinase recombinant rat protein substrate expressed in Escherichia coli, phosphorylation at Ser12, activity of catalytic PKA subunit Zea mays ADP + phosphorylated L-pyruvate kinase
-
?
2.7.11.11 ATP + RRASVA pyruvate kinase-derived peptide substrate comprising the phosphorylation site around Ser12 of the protein, activity of catalytic PKA subunit Zea mays ADP + RRA-phosphoserine-VA
-
?
2.7.11.11 additional information substrate specificity profile utilizing L-pyruvate kinase mutants and pyruvate kinase-derived peptide substrate mutants, mutated to different amino acids at positions 9,10, and 13, as protein substrates, overview Zea mays ?
-
?

Synonyms

EC Number Synonyms Comment Organism
2.7.11.11 PKA
-
Zea mays
2.7.11.11 protein kinase A
-
Zea mays

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.11.11 25
-
assay at Zea mays

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.11.11 7.5
-
assay at Zea mays

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.11 ATP
-
Zea mays