Histidinol-phosphatase
| histidinol-phosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Histidinol-phosphatase tetramer, Thermus thermophilus | |||||||||
| Identifiers | |||||||||
| EC no. | 3.1.3.15 | ||||||||
| CAS no. | 9025-79-0 | ||||||||
| 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 histidinol-phosphatase (EC 3.1.3.15) is an enzyme that catalyzes the chemical reaction
- L-histidinol phosphate + H2O L-histidinol + phosphate
Thus, the two substrates of this enzyme are and H2O, whereas its two products are and phosphate.
This enzyme participates in histidine metabolism.
Nomenclature[]
This enzyme belongs to the family of hydrolases, to be specific, those acting on phosphoric monoester bonds. The systematic name of this enzyme class is L-histidinol-phosphate phosphohydrolase. Other names in common use include histidinol phosphate phosphatase, L-histidinol phosphate phosphatase, histidinolphosphate phosphatase, HPpase, and histidinolphosphatase.
E. coli[]
In E. coli the enzyme encoded by the gene hisB is a fused imidazoleglycerol-phosphate dehydratase and histidinol-phosphatase.[1]
References[]
- ^ Brilli M, Fani R (February 2004). "Molecular evolution of hisB genes". Journal of Molecular Evolution. 58 (2): 225–37. Bibcode:2004JMolE..58..225B. doi:10.1007/s00239-003-2547-x. PMID 15042344. S2CID 1684458.
Further reading[]
- Ames BN (June 1957). "The biosynthesis of histidine; L-histidinol phosphate phosphatase". The Journal of Biological Chemistry. 226 (2): 583–93. PMID 13438843.
- EC 3.1.3
- Enzymes of known structure
- EC 3.1 stubs