Pyridoxal phosphatase
| Pyridoxal phosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.3.74 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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.[1][2][3] Pyridoxal phosphate is an essential cofactor in many other enzyme-catalysed reactions and its cellular concentration is controlled by this hydrolysis.[4] This phosphatase is also found in plants.[5]
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.[6]
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.
References
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ Jeanclos, Elisabeth; Albersen, Monique; Ramos, Rúben J.J.; et al. (2019). "Improved cognition, mild anxiety-like behaviour and decreased motor performance in pyridoxal phosphatase-deficient mice". Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1865 (1): 193–205. doi:10.1016/j.bbadis.2018.08.018. PMID 30327125.
- ↑ Huang, Shuohao; Zhang, Jianyun; Ma, Yaping; Wei, Shu; Huang, Longquan (2012). "Characterization of an acid phosphatase responsible for hydrolysis of pyridoxal 5′-phosphate in tobacco plants". Plant Physiology and Biochemistry. 57: 114–119. doi:10.1016/j.plaphy.2012.05.017. PMID 22698754.
- ↑ Enzyme 3.1.3.74 at KEGG Pathway Database.