KEGG   ENZYME: 1.5.99.4Help
Entry
EC 1.5.99.4                 Enzyme                                 

Name
nicotine dehydrogenase;
nicotine oxidase;
D-nicotine oxidase;
nicotine:(acceptor) 6-oxidoreductase (hydroxylating);
L-nicotine oxidase
Class
Oxidoreductases;
Acting on the CH-NH group of donors;
With other acceptors
BRITE hierarchy
Sysname
nicotine:acceptor 6-oxidoreductase (hydroxylating)
Reaction(IUBMB)
(S)-nicotine + acceptor + H2O = (S)-6-hydroxynicotine + reduced acceptor [RN:R02860]
Reaction(KEGG)
Substrate
(S)-nicotine [CPD:C00745];
acceptor [CPD:C00028];
H2O [CPD:C00001]
Product
(S)-6-hydroxynicotine [CPD:C01056];
reduced acceptor [CPD:C00030]
Comment
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].
History
EC 1.5.99.4 created 1972
Pathway
Nicotinate and nicotinamide metabolism
Microbial metabolism in diverse environments
Reference
1  [PMID:13475371]
  Authors
BEHRMAN EJ, STANIER RY.
  Title
The bacterial oxidation of nicotinic acid.
  Journal
J. Biol. Chem. 228 (1957) 923-45.
  Organism
Pseudomonas fluorescens
Reference
2  [PMID:5849820]
  Authors
Decker K, Bleeg H.
  Title
Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxidans.
  Journal
Biochim. Biophys. Acta. 105 (1965) 313-24.
  Organism
Arthrobacter oxidans
Reference
3  [PMID:4962139]
  Authors
Hochstein LI, Dalton BP.
  Title
The purification and properties of nicotine oxidase.
  Journal
Biochim. Biophys. Acta. 139 (1967) 56-68.
  Organism
Arthrobacter oxidans
Reference
4  [PMID:13610912]
  Authors
HOCHSTEIN LI, RITTENBERG SC.
  Title
The bacterial oxidation of nicotine. II. The isolation of the first oxidative product and its identification as (1)-6-hydroxynicotine.
  Journal
J. Biol. Chem. 234 (1959) 156-60.
  Organism
Corynebacterium nicotinovorum
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 
CAS: 
37256-31-8

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