2,6-dihydroxypyridine 3-monooxygenase

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In enzymology, a 2,6-dihydroxypyridine 3-monooxygenase (EC 1.14.13.10) is an enzyme that catalyzes the chemical reaction

2,6-dihydroxypyridine + NADH + H⁺ + O₂ $\rightleftharpoons$ 2,3,6-trihydroxypyridine + NAD⁺ + H₂O

The 4 substrates of this enzyme are 2,6-dihydroxypyridine, NADH, H⁺, and O₂, whereas its 3 products are 2,3,6-trihydroxypyridine, NAD⁺, and H₂O.

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 one atom o oxygen into the other donor. The systematic name of this enzyme class is 2,6-dihydroxypyridine,NADH:oxygen oxidoreductase (3-hydroxylating). This enzyme is also called 2,6-dihydroxypyridine oxidase. It has 2 cofactors: FAD, and Flavoprotein.

[edit] References

IUBMB entry for 1.14.13.10
BRENDA references for 1.14.13.10 (Recommended.)
PubMed references for 1.14.13.10
PubMed Central references for 1.14.13.10
Google Scholar references for 1.14.13.10
Holmes PE, Rittenberg SC (1972). "The bacterial oxidation of nicotine. VII. Partial purification and properties of 2,6-dihydroxypyridine oxidase". J. Biol. Chem. 247: 7622–7. PMID 4344227.
Holmes PE, Rittenberg SC, Knackmuss HJ (1972). "The bacterial oxidation of nicotine. 8. Synthesis of 2,3,6-trihydroxypyridine and accumulation and partial characterization of the product of 2,6-dihydroxypyridine oxidation". J. Biol. Chem. 247: 7628–33. PMID 4636328.