| 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 | ||||||||
| |||||||||
The enzyme histidinol-phosphatase (EC 3.1.3.15) catalyzes the reaction
- L-histidinol phosphate + H2O L-histidinol + 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 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): 225–237. Bibcode:2004JMolE..58..225B. doi:10.1007/s00239-003-2547-x. PMID 15042344. S2CID 1684458.
Further reading
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