EC 1.14.13.241 - 5-pyridoxate monooxygenase

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IntEnz Enzyme Nomenclature
EC 1.14.13.241

Names

Accepted name:
5-pyridoxate monooxygenase
Other names:
5-pyridoxate oxidase [misleading]
5-pyridoxate,NADPH:oxygen oxidoreductase (decyclizing)
5-pyridoxate dioxygenase [incorrect]
Systematic name:
5-pyridoxate,NADPH:oxygen oxidoreductase (ring-opening)

Reaction

Cofactor

Comments:

Contains FAD. The enzyme, characterized from the bacterium Arthrobacter sp. Cr-7, participates in the degradation of pyridoxine (vitamin B6). Although the enzyme was initially thought to be a dioxygenase, oxygen-tracer experiments have suggested that it is a monooxygnase, incorporating only one oxygen atom from molecular oxygen into the product. The second oxygen atom originates from a water molecule, which is regenerated during the reaction and thus does not show up in the reaction equation.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ERGO , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
CAS Registry Number: 37256-70-5

References

  1. Sparrow, L.G., Ho, P.P.K., Sundaram, T.K., Zach, D., Nyns, E.J. and Snell, E.E.
    The bacterial oxidation of vitamin B6. VII. Purification, properties, and mechanism of action of an oxygenase which cleaves the 3-hydroxypyridine ring.
    J. Biol. Chem. 244: 2590-2600 (1969). [PMID: 4306031]
  2. Nelson, M. J., Snell, E. E.
    Enzymes of vitamin B6 degradation. Purification and properties of 5-pyridoxic-acid oxygenase from Arthrobacter sp.
    J. Biol. Chem. 261: 15115-15120 (1986). [PMID: 3771566]
  3. Chaiyen, P.
    Flavoenzymes catalyzing oxidative aromatic ring-cleavage reactions.
    Arch. Biochem. Biophys. 493: 62-70 (2010). [PMID: 19728986]

[EC 1.14.13.241 created 2018 (EC 1.14.12.5 created 1972, incorporated 2018)]