| EC |
3.1.3.74 |
| Accepted name: |
pyridoxal phosphatase |
| Reaction: |
pyridoxal 5′-phosphate + H2O = pyridoxal + phosphate |
| Other name(s): |
vitamine B6 (pyridoxine) phosphatase; PLP phosphatase; vitamin B6-phosphate phosphatase; PNP phosphatase |
| Systematic name: |
pyridoxal-5′-phosphate phosphohydrolase |
| Comments: |
Requires Mg2+. This enzyme is specific for phosphorylated vitamin B6 compounds: it acts not only on pyridoxal phosphate (PLP), but also on pyridoxine phosphate (PNP), pyridoxamine phosphate (PMP), 4-pyridoxic acid phosphate and 4-deoxypyridoxine phosphate. This reaction can also be carried out by EC 3.1.3.1 (alkaline phosphatase) and EC 3.1.3.2 (acid phosphatase), but these enzymes have very broad substrate specificities. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9076-92-0 |
| References: |
| 1. |
Fonda, M.L. Purification and characterization of vitamin B6-phosphate phosphatase from human erythrocytes. J. Biol. Chem. 267 (1992) 15978–15983. [PMID: 1322411] |
| 2. |
Fonda, M.L. and Zhang, Y.N. Kinetic mechanism and divalent metal activation of human erythrocyte pyridoxal phosphatase. Arch. Biochem. Biophys. 320 (1995) 345–352. [DOI] [PMID: 7625842] |
| 3. |
Jang, Y.M., Kim, D.W., Kang, T.C., Won, M.H., Baek, N.I., Moon, B.J., Choi, S.Y. and Kwon, O.S. Human pyridoxal phosphatase. Molecular cloning, functional expression, and tissue distribution. J. Biol. Chem. 278 (2003) 50040–50046. [DOI] [PMID: 14522954] |
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| [EC 3.1.3.74 created 2004] |
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