KEGG   ENZYME: 1.5.3.6Help
Entry
EC 1.5.3.6                  Enzyme                                 

Name
(R)-6-hydroxynicotine oxidase;
D-6-hydroxynicotine oxidase;
6-hydroxy-D-nicotine oxidase
Class
Oxidoreductases;
Acting on the CH-NH group of donors;
With oxygen as acceptor
BRITE hierarchy
Sysname
(R)-6-hydroxynicotine:oxygen oxidoreductase
Reaction(IUBMB)
(R)-6-hydroxynicotine + H2O + O2 = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2 (overall reaction) [RN:R07170];
(1a) (R)-6-hydroxynicotine + O2 = 5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol + H2O2  [RN:R11050];
(1b) 5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol + H2O = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one (spontaneous) [RN:R11049]
Reaction(KEGG)
Substrate
(R)-6-hydroxynicotine [CPD:C03043];
H2O [CPD:C00001];
O2 [CPD:C00007];
5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol [CPD:C21075]
Product
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one [CPD:C01297];
H2O2 [CPD:C00027];
5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol [CPD:C21075]
Comment
A flavoprotein (FAD). The enzyme, which participates in nicotine degradation, is specific for (R) isomer of 6-hydroxynicotine, derived from the uncommon (R)-nicotine. The bacterium Arthrobacter nicotinovorans, in which this enzyme was originally discovered, has a different enzyme that catalyses a similar reaction with the (S)-isomer (cf. EC 1.5.3.5, (S)-6-hydroxynicotine oxidase).
History
EC 1.5.3.6 created 1972, modified 2015
Pathway
ec00760  Nicotinate and nicotinamide metabolism
ec01120  Microbial metabolism in diverse environments
Orthology
K19890  (R)-6-hydroxynicotine oxidase
Reference
1  [PMID:5849820]
  Authors
Decker K, Bleeg H.
  Title
Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxidans.
  Journal
Biochim Biophys Acta 105:313-24 (1965)
Reference
2  [PMID:4628374]
  Authors
Bruhmuller M, Mohler H, Decker K.
  Title
Covalently bound flavin in D-6-hydroxynicotine oxidase from Arthrobacter oxidans. Purification and properties of D-6-hydroxynicotine oxidase.
  Journal
Eur J Biochem 29:143-51 (1972)
DOI:10.1111/j.1432-1033.1972.tb01968.x
Reference
3  [PMID:3622516]
  Authors
Brandsch R, Hinkkanen AE, Mauch L, Nagursky H, Decker K
  Title
6-Hydroxy-D-nicotine oxidase of Arthrobacter oxidans. Gene structure of the flavoenzyme and its relationship to 6-hydroxy-L-nicotine oxidase.
  Journal
Eur J Biochem 167:315-20 (1987)
DOI:10.1111/j.1432-1033.1987.tb13338.x
Reference
4  [PMID:9878353]
  Authors
Schenk S, Hoelz A, Krauss B, Decker K
  Title
Gene structures and properties of enzymes of the plasmid-encoded nicotine catabolism of Arthrobacter nicotinovorans.
  Journal
J Mol Biol 284:1323-39 (1998)
DOI:10.1006/jmbi.1998.2227
Reference
5  [PMID:16095622]
  Authors
Koetter JW, Schulz GE
  Title
Crystal structure of 6-hydroxy-D-nicotine oxidase from Arthrobacter nicotinovorans.
  Journal
J Mol Biol 352:418-28 (2005)
DOI:10.1016/j.jmb.2005.07.041
Other DBs
ExplorEnz - The Enzyme Database: 1.5.3.6
IUBMB Enzyme Nomenclature: 1.5.3.6
ExPASy - ENZYME nomenclature database: 1.5.3.6
UM-BBD (Biocatalysis/Biodegradation Database): 1.5.3.6
BRENDA, the Enzyme Database: 1.5.3.6
CAS: 37233-46-8

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