The Enzyme Database

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EC 1.5.3.5     
Accepted name: (S)-6-hydroxynicotine oxidase
Reaction: (S)-6-hydroxynicotine + H2O + O2 = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2 (overall reaction)
(1a) (S)-6-hydroxynicotine + O2 = 5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol + H2O2
(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)
For diagram of nicotine catabolism by arthrobacter, click here
Glossary: (S)-6-hydroxynicotine = 5-[(2S)-1-methylpyrrolidin-2-yl]pyridin-2-ol
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 6-hydroxypseudooxynicotine
5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol = 6-hydroxy-N-methylmyosmine
Other name(s): L-6-hydroxynicotine oxidase; 6-hydroxy-L-nicotine oxidase; 6-hydroxy-L-nicotine:oxygen oxidoreductase; nctB (gene name)
Systematic name: (S)-6-hydroxynicotine:oxygen oxidoreductase
Comments: A flavoprotein (FAD). The enzyme, which participates in nicotine degradation, is specific for the (S) isomer of 6-hydroxynicotine. The bacterium Arthrobacter nicotinovorans, in which this enzyme was originally discovered, has a different enzyme that catalyses a similar reaction with the less common (R)-isomer (cf. EC 1.5.3.6, (R)-6-hydroxynicotine oxidase).
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-29-4
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.  Dai, V.D., Decker, K. and Sund, H. Purification and properties of L-6-hydroxynicotine oxidase. Eur. J. Biochem. 4 (1968) 95–102. [DOI] [PMID: 5646150]
3.  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]
4.  Qiu, J., Wei, Y., Ma, Y., Wen, R., Wen, Y. and Liu, W. A novel (S)-6-hydroxynicotine oxidase gene from Shinella sp. strain HZN7. Appl. Environ. Microbiol. 80 (2014) 5552–5560. [DOI] [PMID: 25002425]
[EC 1.5.3.5 created 1972, modified 2015]
 
 
EC 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-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol + H2O2
(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)
For diagram of nicotine catabolism by arthrobacter, click here
Glossary: (R)-6-hydroxynicotine = 5-[(2R)-1-methylpyrrolidin-2-yl]pyridin-2-ol
5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol = 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 (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, 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]
[EC 1.5.3.6 created 1972, modified 2015]
 
 
EC 1.5.99.14     
Accepted name: 6-hydroxypseudooxynicotine dehydrogenase
Reaction: 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + acceptor + H2O = 1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one + reduced acceptor
For diagram of nicotine catabolism by arthrobacter, click here
Glossary: 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 6-hydroxypseudooxynicotine
1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 2,6-dihydroxypseudooxynicotine
Systematic name: 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one:acceptor 6-oxidoreductase (hydroxylating)
Comments: Contains a cytidylyl molybdenum cofactor [3]. The enzyme, which participates in the nicotine degradation pathway, has been characterized from the soil bacterium Arthrobacter nicotinovorans [1,2].
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Freudenberg, W., Konig, K. and Andreesen, J. R. Nicotine dehydrogenase from Arthrobacter oxidans: A molybdenum-containing hydroxylase. FEMS Microbiology Letters 52 (1988) 13–18.
2.  Grether-Beck, S., Igloi, G.L., Pust, S., Schilz, E., Decker, K. and Brandsch, R. Structural analysis and molybdenum-dependent expression of the pAO1-encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans. Mol. Microbiol. 13 (1994) 929–936. [DOI] [PMID: 7815950]
3.  Sachelaru, P., Schiltz, E. and Brandsch, R. A functional mobA gene for molybdopterin cytosine dinucleotide cofactor biosynthesis is required for activity and holoenzyme assembly of the heterotrimeric nicotine dehydrogenases of Arthrobacter nicotinovorans. Appl. Environ. Microbiol. 72 (2006) 5126–5131. [DOI] [PMID: 16820521]
[EC 1.5.99.14 created 2012]
 
 


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