| EC |
1.5.99.4 |
| Accepted name: |
nicotine 6-hydroxylase |
| Reaction: |
(S)-nicotine + acceptor + H2O = (S)-6-hydroxynicotine + reduced acceptor |
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For diagram of nicotine catabolism by arthrobacter, click here |
| Other name(s): |
nicotine oxidase; D-nicotine oxidase; nicotine:(acceptor) 6-oxidoreductase (hydroxylating); L-nicotine oxidase; nicotine dehydrogenase (incorrect) |
| Systematic name: |
nicotine:acceptor 6-oxidoreductase (hydroxylating) |
| Comments: |
A metalloprotein (FMN). The enzyme can act on both the naturally found (S)-enantiomer and the synthetic (R)-enantiomer of nicotine, with retention of configuration in both cases [4]. |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 37256-31-8 |
| References: |
| 1. |
Behrman, E.J. and Stanier, R.Y. The bacterial oxidation of nicotinic acid. J. Biol. Chem. 228 (1957) 923–945. [PMID: 13475371] |
| 2. |
Decker, K. and Bleeg, H. Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxidans. Biochim. Biophys. Acta 105 (1965) 313–324. [PMID: 5849820] |
| 3. |
Hochstein, L.I. and Dalton, B.P. The purification and properties of nicotine oxidase. Biochim. Biophys. Acta 139 (1967) 56–68. [DOI] [PMID: 4962139] |
| 4. |
Hochstein, L.I. and Rittenberg, S.C. The bacterial oxidation of nicotine. II. The isolation of the first oxidative product and its identification as (1)-6-hydroxynicotine. J. Biol. Chem. 234 (1959) 156–160. [PMID: 13610912] |
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| [EC 1.5.99.4 created 1972, modified 2023] |
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