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Literature summary for 2.7.11.11 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
Search for more literature for 2.7.11.11

Activating Compound

Activating Compound Comment Organism Structure
cAMP dependent on Zea mays

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
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
-
 ?
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

Synonyms Comment Organism
PKA
-
 Zea mays
protein kinase A
-
 Zea mays

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Zea mays