ExplorEnz: EC 1.5.3.6

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1.5.3.6

Accepted name:

(R)-6-hydroxynicotine oxidase

Reaction:

(R)-6-hydroxynicotine + H₂O + O₂ = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H₂O₂ (overall reaction)
(1a) (R)-6-hydroxynicotine + O₂ = 5-(6-hydroxypyridin-3-yl)-1-methyl-3,4-dihydro-2H-pyrrol-1-ium + H₂O₂
(1b) 5-(6-hydroxypyridin-3-yl)-1-methyl-3,4-dihydro-2H-pyrrol-1-ium + H₂O = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one (spontaneous)

For diagram of nicotine catabolism by arthrobacter, click here

Glossary:

(R)-6-hydroxynicotine = 5-[(2R)-1-methylpyrrolidin-2-yl]pyridin-2-ol
5-(6-hydroxypyridin-3-yl)-1-methyl-3,4-dihydro-2H-pyrrol-1-ium = 6-hydroxy-N-methylmyosmine
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 6-hydroxypseudooxynicotine

Other name(s):

D-6-hydroxynicotine oxidase; 6-hydroxy-D-nicotine oxidase

Systematic name:

(R)-6-hydroxynicotine:oxygen oxidoreductase

Comments:

A flavoprotein (FAD). The enzyme, which participates in nicotine degradation, is specific for the (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).

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, GENE, KEGG, MetaCyc, PDB, CAS registry number: 37233-46-8

References:

1.	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]
2.	Brühmüller, M., Möhler, H.K. and Decker, K. Covalently bound flavin in D-6-hydroxynicotine oxidase from Arthrobacter oxidans. Purification and properties of D-6-hydroxynicotine oxidase. Eur. J. Biochem. 29 (1972) 143–151. [DOI] [PMID: 4628374]
3.	Brandsch, R., Hinkkanen, A.E., Mauch, L., Nagursky, H. and Decker, K. 6-Hydroxy-D-nicotine oxidase of Arthrobacter oxidans. Gene structure of the flavoenzyme and its relationship to 6-hydroxy-L-nicotine oxidase. Eur. J. Biochem. 167 (1987) 315–320. [DOI] [PMID: 3622516]
4.	Schenk, S., Hoelz, A., Krauss, B. and Decker, K. Gene structures and properties of enzymes of the plasmid-encoded nicotine catabolism of Arthrobacter nicotinovorans. J. Mol. Biol. 284 (1998) 1323–1339. [DOI] [PMID: 9878353]
5.	Koetter, J.W. and Schulz, G.E. Crystal structure of 6-hydroxy-D-nicotine oxidase from Arthrobacter nicotinovorans. J. Mol. Biol. 352 (2005) 418–428. [DOI] [PMID: 16095622]
6.	Fitzpatrick, P.F., Chadegani, F., Zhang, S., Roberts, K.M. and Hinck, C.S. Mechanism of the flavoprotein L-hydroxynicotine oxidase: kinetic mechanism, substrate specificity, reaction product, and roles of active-site residues. Biochemistry 55 (2016) 697–703. [DOI] [PMID: 26744768]

[EC 1.5.3.6 created 1972, modified 2015]