(R)-6-hydroxynicotine oxidase

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In enzymology, a (R)-6-hydroxynicotine oxidase (EC 1.5.3.6) is an enzyme that catalyzes the chemical reaction

(R)-6-hydroxynicotine + H₂O + O₂ $\rightleftharpoons$ 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H₂O₂

The 3 substrates of this enzyme are (R)-6-hydroxynicotine, H₂O, and O₂, whereas its two products are 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one and H₂O₂.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with oxygen as acceptor. The systematic name of this enzyme class is (R)-6-hydroxynicotine:oxygen oxidoreductase. Other names in common use include D-6-hydroxynicotine oxidase, and 6-hydroxy-D-nicotine oxidase. It employs one cofactor, FAD.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2BVF, 2BVG, and 2BVH.

[edit] References

IUBMB entry for 1.5.3.6
BRENDA references for 1.5.3.6 (Recommended.)
PubMed references for 1.5.3.6
PubMed Central references for 1.5.3.6
Google Scholar references for 1.5.3.6
Bruhmuller M, Mohler H, Decker K (1972). "Covalently bound flavin in D-6-hydroxynicotine oxidase from Arthrobacter oxidans. Purification and properties of D-6-hydroxynicotine oxidase". Eur. J. Biochem. 29: 143–51. doi:10.1111/j.1432-1033.1972.tb01968.x. PMID 4628374.
Decker K, Bleeg H (1965). "Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxidans". Biochim. Biophys. Acta. 105: 313–24. PMID 5849820.