Pyridoxal phosphatase
| Pyridoxal phosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.1.3.74 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a pyridoxal phosphatase (EC 3.1.3.74) is an enzyme that catalyzes the chemical reaction
- pyridoxal 5'-phosphate + H2O pyridoxal + phosphate
Thus, the two substrates of this enzyme are pyridoxal 5'-phosphate and H2O, whereas its two products are pyridoxal 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 pyridoxal-5'-phosphate phosphohydrolase. Other names in common use include vitamine B6 (pyridoxine) phosphatase, PLP phosphatase, vitamin B6-phosphate phosphatase, and PNP phosphatase. This enzyme participates in vitamin B6 metabolism.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 2CFR, 2CFS, 2CFT, 2OYC, 2P27, and 2P69.
References
- Fonda ML (1992). "Purification and characterization of vitamin B6-phosphate phosphatase from human erythrocytes". J. Biol. Chem. 267 (22): 15978–83. PMID 1322411.
- Fonda ML, Zhang YN (1995). "Kinetic mechanism and divalent metal activation of human erythrocyte pyridoxal phosphatase". Arch. Biochem. Biophys. 320 (2): 345–52. PMID 7625842. doi:10.1016/0003-9861(95)90018-7.
- OS; Kim, DW; Kang, TC; Won, MH; Baek, NI; Moon, BJ; Choi, SY; Kwon, OS (2003). "Human pyridoxal phosphatase. Molecular cloning, functional expression, and tissue distribution". J. Biol. Chem. 278 (50): 50040–6. PMID 14522954. doi:10.1074/jbc.M309619200.