In enzymology, a nicotine dehydrogenase (EC 1.5.99.4) is an enzyme that catalyzes the chemical reaction
| nicotine dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.5.99.4 | ||||||||
| CAS no. | 37256-31-8 | ||||||||
| 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 | ||||||||
| |||||||||
- (S)-nicotine + acceptor + H2O (S)-6-hydroxynicotine + reduced acceptor
The 3 substrates of this enzyme are (S)-nicotine, acceptor, and H2O, whereas its two products are (S)-6-hydroxynicotine and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other acceptors. The systematic name of this enzyme class is nicotine:acceptor 6-oxidoreductase (hydroxylating). Other names in common use include nicotine oxidase, D-nicotine oxidase, nicotine:(acceptor) 6-oxidoreductase (hydroxylating), and L-nicotine oxidase. It has 2 cofactors: metal, and FMN.
References
edit- BEHRMAN EJ, STANIER RY (1957). "The bacterial oxidation of nicotinic acid". J. Biol. Chem. 228 (2): 923–45. PMID 13475371.
- 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.
- Hochstein LI, Dalton BP (1967). "The purification and properties of nicotine oxidase". Biochim. Biophys. Acta. 139 (1): 56–68. doi:10.1016/0005-2744(67)90113-1. PMID 4962139.
- HOCHSTEIN LI, RITTENBERG SC (1959). "The bacterial oxidation of nicotine. II. The isolation of the first oxidative product and its identification as (1)-6-hydroxynicotine". J. Biol. Chem. 234 (1): 156–60. PMID 13610912.
