| protein histidine pros-kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.13.1 | ||||||||
| CAS no. | 99283-67-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a protein-histidine pros-kinase (EC 2.7.13.1) is an enzyme that catalyzes the chemical reaction
- ATP + protein L-histidine ADP + protein Nπ-phospho-L-histidine
Thus, the two substrates of this enzyme are ATP and protein L-histidine, whereas its two products are ADP and protein Npi-phospho-L-histidine.
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain of histidine residues in proteins (protein-histidine kinases). The systematic name of this enzyme class is ATP:protein-L-histidine Npi-phosphotransferase. Other names in common use include ATP:protein-L-histidine N-pros-phosphotransferase, histidine kinase, histidine protein kinase, protein histidine kinase, protein kinase (histidine), and HK2.
References[edit]
- Fujitaki JM, Fung G, Oh EY, Smith RA (1981). "Characterization of chemical enzymatic acid-labile phosphorylation of histone H4 using phosphorus-31 nuclear magnetic resonance". Biochemistry. 20 (12): 3658–64. doi:10.1021/bi00515a055. PMID 7196259.
- Huebner VD, Matthews HR (1985). "Phosphorylation of histidine in proteins by a nuclear extract of Physarum polycephalum plasmodia". J. Biol. Chem. 260 (30): 16106–13. PMID 4066704.
