5-pyridoxate dioxygenase

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In enzymology, a 5-pyridoxate dioxygenase (EC 1.14.12.5) is an enzyme that catalyzes the chemical reaction

3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate + NADPH + H⁺ + O₂ $\rightleftharpoons$ 2-(acetamidomethylene)-3-(hydroxymethyl)succinate + NADP⁺

The 4 substrates of this enzyme are 3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate, NADPH, H⁺, and O₂, whereas its two products are 2-(acetamidomethylene)-3-(hydroxymethyl)succinate and NADP⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is 5-pyridoxate,NADPH:oxygen oxidoreductase (decyclizing). This enzyme is also called 5-pyridoxate oxidase. This enzyme participates in vitamin b6 metabolism. It has 2 cofactors: FAD, and Flavoprotein.

[edit] References

IUBMB entry for 1.14.12.5
BRENDA references for 1.14.12.5 (Recommended.)
PubMed references for 1.14.12.5
PubMed Central references for 1.14.12.5
Google Scholar references for 1.14.12.5
Sparrow LG, Ho PP, Sundaram TK, Zach D, Nyns EJ, Snell EE (1969). "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: 2590–600. PMID 4306031.