In enzymology, a senecionine N-oxygenase (EC 1.14.13.101) is an enzyme that catalyzes the chemical reaction
| Senecionine N-oxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.101 | ||||||||
| CAS no. | 220581-68-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- senecionine + NADPH + H+ + O2 senecionine N-oxide + NADP+ + H2O
The 4 substrates of this enzyme are senecionine, NADPH, H+, and O2, whereas its 3 products are senecionine N-oxide, 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 senecionine,NADPH:oxygen oxidoreductase (N-oxide-forming). Other names in common use include senecionine monooxygenase (N-oxide-forming) and SNO.
References
edit- Lindigkeit R, Biller A, Buch M, Schiebel HM, Boppre M, Hartmann T (1997). "The two facies of pyrrolizidine alkaloids: the role of the tertiary amine and its N-oxide in chemical defense of insects with acquired plant alkaloids". Eur. J. Biochem. 245 (3): 626–36. doi:10.1111/j.1432-1033.1997.00626.x. PMID 9182998.
- Naumann C, Hartmann T, Ober D (2002). "Evolutionary recruitment of a flavin-dependent monooxygenase for the detoxification of host plant-acquired pyrrolizidine alkaloids in the alkaloid-defended arctiid moth Tyria jacobaeae". Proc. Natl. Acad. Sci. U.S.A. 99 (9): 6085–90. Bibcode:2002PNAS...99.6085N. doi:10.1073/pnas.082674499. PMC 122906. PMID 11972041.
