EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
2.7.11.11 | cAMP | dependent on | Zea mays |
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 |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.11.11 | Mg2+ | - |
Zea mays |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.11.11 | Zea mays | - |
- |
- |
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 | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.7.11.11 | PKA | - |
Zea mays |
2.7.11.11 | protein kinase A | - |
Zea mays |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.7.11.11 | 25 | - |
assay at | Zea mays |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.7.11.11 | 7.5 | - |
assay at | Zea mays |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.7.11.11 | ATP | - |
Zea mays |