Kynurenine 3-monooxygenase

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In enzymology, a kynurenine 3-monooxygenase (EC 1.14.13.9) is an enzyme that catalyzes the chemical reaction

L-kynurenine + NADPH + H⁺ + O₂ $\rightleftharpoons$ 3-hydroxy-L-kynurenine + NADP⁺ + H₂O

The 4 substrates of this enzyme are L-kynurenine, NADPH, H⁺, and O₂, whereas its 3 products are 3-hydroxy-L-kynurenine, NADP⁺, 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 L-kynurenine,NADPH:oxygen oxidoreductase (3-hydroxylating). Other names in common use include kynurenine 3-hydroxylase, kynurenine hydroxylase, and L-kynurenine-3-hydroxylase. This enzyme participates in tryptophan metabolism. It employs one cofactor, FAD.

[edit] References

IUBMB entry for 1.14.13.9
BRENDA references for 1.14.13.9 (Recommended.)
PubMed references for 1.14.13.9
PubMed Central references for 1.14.13.9
Google Scholar references for 1.14.13.9
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Okamoto H, Hayaishi O (1967). "Flavin adenine dinucleotide requirement for kynurenine hydroxylase of rat liver mitochondria". Biochem. Biophys. Res. Commun. 29: 394–9. doi:10.1016/0006-291X(67)90469-X. PMID 6076241.
SAITO Y, HAYAISHI O, ROTHBERG S (1957). "Studies on oxygenases; enzymatic formation of 3-hydroxy-L-kynurenine from L-kynurenine". J. Biol. Chem. 229: 921–34. PMID 13502353.