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The enzyme pyridoxal phosphatase (EC 3.1.3.74) catalyzes the reaction

pyridoxal 5′-phosphate + H₂O ${\displaystyle \rightleftharpoons }$ pyridoxal + phosphate

This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name 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

1. Fonda ML (1992). "Purification and characterization of vitamin B₆-phosphate phosphatase from human erythrocytes". J. Biol. Chem. 267 (22): 15978–83. doi:10.1016/S0021-9258(19)49630-0. PMID 1322411.
2. Fonda ML, Zhang YN (1995). "Kinetic mechanism and divalent metal activation of human erythrocyte pyridoxal phosphatase". Arch. Biochem. Biophys. 320 (2): 345–52. doi:10.1016/0003-9861(95)90018-7. PMID 7625842.
3. Jang, Y.M.; 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. doi:10.1074/jbc.M309619200. PMID 14522954.

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