Nicotine dehydrogenase

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In enzymology, a nicotine dehydrogenase (EC 1.5.99.4) is an enzyme that catalyzes the chemical reaction

(S)-nicotine + acceptor + H₂O $\rightleftharpoons$ (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.

[edit] References

IUBMB entry for 1.5.99.4
BRENDA references for 1.5.99.4 (Recommended.)
PubMed references for 1.5.99.4
PubMed Central references for 1.5.99.4
Google Scholar references for 1.5.99.4
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Decker K, Bleeg H (1965). "Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxidans". Biochim. Biophys. Acta. 105: 313–24. PMID 5849820.
Hochstein LI, Dalton BP (1967). "The purification and properties of nicotine oxidase". Biochim. Biophys. Acta. 139: 56–68. 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: 156–60. PMID 13610912.