Acting on the CH-NH group of donors;
With oxygen as acceptor
(R)-6-hydroxynicotine + H2O + O2 = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2 (overall reaction) [RN:
(1a) (R)-6-hydroxynicotine + O2 = 5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol + H2O2 [RN:
(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:
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
, (S)-6-hydroxynicotine oxidase).
EC 188.8.131.52 created 1972, modified 2015
ec00760 Nicotinate and nicotinamide metabolism
ec01120 Microbial metabolism in diverse environments
K19890 (R)-6-hydroxynicotine oxidase
Decker K, Bleeg H.
Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxidans.
Bruhmuller M, Mohler H, Decker K.
Covalently bound flavin in D-6-hydroxynicotine oxidase from Arthrobacter oxidans. Purification and properties of D-6-hydroxynicotine oxidase.
Brandsch R, Hinkkanen AE, Mauch L, Nagursky H, Decker K
6-Hydroxy-D-nicotine oxidase of Arthrobacter oxidans. Gene structure of the flavoenzyme and its relationship to 6-hydroxy-L-nicotine oxidase.
Schenk S, Hoelz A, Krauss B, Decker K
Gene structures and properties of enzymes of the plasmid-encoded nicotine catabolism of Arthrobacter nicotinovorans.
Koetter JW, Schulz GE
Crystal structure of 6-hydroxy-D-nicotine oxidase from Arthrobacter nicotinovorans.
ExplorEnz - The Enzyme Database: 184.108.40.206
ExPASy - ENZYME nomenclature database: 220.127.116.11
UM-BBD (Biocatalysis/Biodegradation Database): 18.104.22.168
BRENDA, the Enzyme Database: 22.214.171.124