EC - 5-pyridoxate monooxygenase

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IntEnz Enzyme Nomenclature


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)




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


  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 created 2018 (EC created 1972, incorporated 2018)]