The enzyme pyridoxal phosphatase (EC 3.1.3.74) catalyzes the reaction
The enzyme characterised from human erythrocytes hydrolyses pyridoxal phosphate to pyridoxal and orthophosphate. Pyridoxal phosphate is an essential cofactor in many other enzyme-catalysed reactions and its cellular concentration is controlled by this hydrolysis. This phosphatase is also found in plants. The enzyme also acts on pyridoxine phosphate, pyridoxamine phosphate, 4-pyridoxic acid phosphate and 4-deoxypyridoxine phosphate to remove their phosphate groups. Two human genes produce proteins that act as this kind of enzyme: PDXP and PHOSPHO2. This enzyme is a hydrolase, specifically one 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.
Structural studies As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes PDB: 2CFR, PDB: 2CFS, PDB: 2CFT, PDB: 2OYC, PDB: 2P27, and PDB: 2P69.
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