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
Main article: hisBIn E. coli the enzyme encoded by the gene hisB is a fused imidazoleglycerol-phosphate dehydratase and histidinol-phosphatase.
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
- Ames BN (June 1957). "The biosynthesis of histidine; L-histidinol phosphate phosphatase". The Journal of Biological Chemistry. 226 (2): 583–593. doi:10.1016/S0021-9258(18)70840-5. PMID 13438843.
Enzymes | |
---|---|
Activity | |
Regulation | |
Classification | |
Kinetics | |
Types |
|
This EC 3.1 enzyme-related article is a stub. You can help Misplaced Pages by expanding it. |