| (R)-6-hydroxynicotine oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.5.3.6 | ||||||||
| CAS no. | 37233-46-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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 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.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2BVF, 2BVG, and 2BVH.
References
- 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 (1): 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 (2): 313–24. doi: 10.1016/s0926-6593(65)80155-2. PMID 5849820.
