EC Number |
Reaction |
Reference |
---|
2.7.11.1 | ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate |
- |
- |
2.7.11.1 | ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate |
active site and activation loop structure and conformation, Lys233, Cys250, Asp368, and Thr386 are important for activity, the substrate binding groove determines the substrate specificity via residues Val318 and Ala448 |
663401 |
2.7.11.1 | ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate |
active site structure |
662128 |
2.7.11.1 | ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate |
catalytic mechanism and regulation of PKN |
662053 |
2.7.11.1 | ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate |
glycogen synthase kinase-3beta also performs the tau-protein kinase reaction, EC 2.7.11.26 |
662127 |
2.7.11.1 | ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate |
Lys45 is important for PknH catalytic and autophosphorylation activity |
661782 |
2.7.11.1 | ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate |
the CK1 family shows a strong preference both in vitro and in vivo for primed, pre-phosphorylated substrates. CK1 family members prefer acidic substrates in vitro, most notably those with acidic residues in the N-3 position, e.g. D-X-X-S/T. The most effective motif contains a phospho-residue in the N-3 position, such as pS/pT-X-X-S/T, where pS/pT refers to a phospho-serine or phospho-threonine, X refers to any amino acid, and the underlined residues refer to the target site |
722389 |
2.7.11.1 | ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate |
the enzyme shows Mn2+-dependent serine/threonine kinase and Ca2+-dependent histidine kinase, EC 2.7.13.3, activities |
663129 |