EC 3.1.3.74 - Pyridoxal phosphatase

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IntEnz Enzyme Nomenclature
EC 3.1.3.74

Names

Accepted name:
pyridoxal phosphatase
Other names:
PLP phosphatase
PNP phosphatase
vitamin B6-phosphate phosphatase
vitamine B6 (pyridoxine) phosphatase
vitamin B6-phosphate phosphatase
vitamine B6 (pyridoxine) phosphatase
Systematic name:
pyridoxal-5'-phosphate phosphohydrolase

Reactions

Cofactor

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0033883
UniProtKB/Swiss-Prot: (11) [show] [UniProt]

References

  1. Fonda, M.L.
    Purification and characterization of vitamin B6-phosphate phosphatase from human erythrocytes.
    J. Biol. Chem. 267: 15978-15983 (1992). [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: 345-352 (1995). [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: 50040-50046 (2003). [PMID: 14522954]

[EC 3.1.3.74 created 2004]