Histidinol-phosphatase
From Wikipedia, the free encyclopedia
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 L-histidinol phosphate and H2O, whereas its two products are L-histidinol and phosphate.
This enzyme belongs to the family of hydrolases, specifically 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. This enzyme participates in histidine metabolism.
Contents[hide] |
[edit] Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 2FPR, 2FPS, 2FPU, 2FPW, and 2FPX.
[edit] References
- IUBMB entry for 3.1.3.15
- BRENDA references for 3.1.3.15 (Recommended.)
- PubMed references for 3.1.3.15
- PubMed Central references for 3.1.3.15
- Google Scholar references for 3.1.3.15
- AMES BN (1957). "The biosynthesis of histidine; L-histidinol phosphate phosphatase". J. Biol. Chem. 226: 583–93. PMID 13438843.
[edit] External links
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- The CAS registry number for this enzyme class is 9025-79-0.