| EC |
1.14.13.241 |
| Accepted name: |
5-pyridoxate monooxygenase |
| Reaction: |
3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate + NADPH + H+ + O2 = 2-(acetamidomethylene)-3-(hydroxymethyl)succinate + NADP+ |
| Glossary: |
3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate = 5-pyridoxate |
| Other name(s): |
5-pyridoxate,NADPH:oxygen oxidoreductase (decyclizing); 5-pyridoxate oxidase (misleading); 5-pyridoxate dioxygenase (incorrect) |
| Systematic name: |
5-pyridoxate,NADPH:oxygen oxidoreductase (ring-opening) |
| 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 monooxygenase, 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: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, 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 (1969) 2590–2600. [PMID: 4306031] |
| 2. |
Nelson, M.J. and Snell, E.E. Enzymes of vitamin B6 degradation. Purification and properties of 5-pyridoxic-acid oxygenase from Arthrobacter sp. J. Biol. Chem. 261 (1986) 15115–15120. [PMID: 3771566] |
| 3. |
Chaiyen, P. Flavoenzymes catalyzing oxidative aromatic ring-cleavage reactions. Arch. Biochem. Biophys. 493 (2010) 62–70. [DOI] [PMID: 19728986] |
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| [EC 1.14.13.241 created 2018 (EC 1.14.12.5 created 1972, incorporated 2018)] |
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