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(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
(S)-6-hydroxynicotine + H2O + O2
6-hydroxy-pseudooxynicotine + H2O2
(S)-6-hydroxynornicotine + H2O + O2
?
-
-
-
-
?
(S)-nicotine + H2O + O2
N-methylmyosmine + H2O2
the enzyme converts (S)-nicotine into N-methylmyosmine, which spontaneously hydrolyzes into pseudooxynicotine
-
-
?
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
-
-
-
-
?
6-hydroxy-L-nicotine + H2O + O2
6-hydroxy-N-methylmyosmine + NH3 + H2O2
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
-
?
L-6-hydroxy-nor-nicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-aminobutan-1-one + H2O2
-
-
-
-
?
additional information
?
-
(S)-6-hydroxynicotine + H2O + O2

1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
transitional product is 6-hydroxy-N-methylmyosmine that hydrolyses spontaneously
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
transitional product is 6-hydroxy-N-methylmyosmine that hydrolyses spontaneously
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
transitional product is 6-hydroxy-N-methylmyosmine that hydrolyses spontaneously
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
transitional product is 6-hydroxy-N-methylmyosmine that hydrolyses spontaneously
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2

1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
-
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
-
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
the enzyme is involved in degradation of nicotine
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
absolute stereospecificity on the L-form
intermediate product 6-hydroxy-N-methylmyosmine, which hydrolyzes to 6-hydroxy-pseudooxynicotine
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
-
the enzyme catalyzes the oxidation of (S)-6-hydroxynicotine to 6-hydroxypseudooxynicotine during microbial catabolism of nicotine
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
-
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
the enzyme is essential for nicotine or (S)-6-hydroxynicotine degradation
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
the enzyme converts (S)-6-hydroxynicotine into 6-hydroxy-N-methylmyosmine which then spontaneously hydrolyzes into 6-hydroxypseudooxynicotine. (S)-6-Hydroxynicotine is the preferred substrate in vivo. The enzyme shows no activities toward the R enantiomer of nicotine or 6-hydroxynicotine
-
-
?
(S)-6-hydroxynicotine + H2O + O2

6-hydroxy-pseudooxynicotine + H2O2
-
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
6-hydroxy-pseudooxynicotine + H2O2
-
-
-
-
?
additional information

?
-
-
transformation of 6-hydroxy-L-nicotine to 6-hydroxy-N-methylmyosmine, 6-hydroxypseudooxynicotine formation, overview
-
-
?
additional information
?
-
-
measurement of enzyme activity using dichlorindophenol. 6-Hydroxypseudooxynicotine forms from 6-hydroxy-N-methylmyosmine non-enzymatically
-
-
?
additional information
?
-
-
transformation of 6-hydroxy-L-nicotine to 6-hydroxy-N-methylmyosmine, 6-hydroxypseudooxynicotine formation, overview
-
-
?
additional information
?
-
-
measurement of enzyme activity using dichlorindophenol. 6-Hydroxypseudooxynicotine forms from 6-hydroxy-N-methylmyosmine non-enzymatically
-
-
?
additional information
?
-
-
also oxidizes circular secondary and tertiary amines
-
-
?
additional information
?
-
-
enzyme production is induced by growing cells in D,L-nicotine as only source of carbon and nitrogen
-
-
?
additional information
?
-
-
enzyme production is induced by growing cells in D,L-nicotine as only source of carbon and nitrogen
-
-
?
additional information
?
-
-
enzyme production is induced by growing cells in D,L-nicotine as only source of carbon and nitrogen
-
-
?
additional information
?
-
-
it is synthesized only during the logarithmic and stationary phases of growth
-
-
?
additional information
?
-
-
no activity with 6-hydroxy-D-nicotine
-
-
?
additional information
?
-
-
synthesis of 6-hydroxy-N-methylmyosmine and 6-hydroxy-pseudooxynicotine from 6-hydroxy-L-nicotine. 6-Hydroxypseudooxynicotine forms from 6-hydroxy-N-methylmyosmine non-enzymatically
-
-
?
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(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
6-hydroxy-L-nicotine + H2O + O2
6-hydroxy-N-methylmyosmine + NH3 + H2O2
-
-
-
-
?
additional information
?
-
(S)-6-hydroxynicotine + H2O + O2

1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
transitional product is 6-hydroxy-N-methylmyosmine that hydrolyses spontaneously
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
transitional product is 6-hydroxy-N-methylmyosmine that hydrolyses spontaneously
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
transitional product is 6-hydroxy-N-methylmyosmine that hydrolyses spontaneously
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
transitional product is 6-hydroxy-N-methylmyosmine that hydrolyses spontaneously
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2

1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
-
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
-
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
the enzyme is involved in degradation of nicotine
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
-
absolute stereospecificity on the L-form
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
-
the enzyme catalyzes the oxidation of (S)-6-hydroxynicotine to 6-hydroxypseudooxynicotine during microbial catabolism of nicotine
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
absolute stereospecificity on the L-form
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
the enzyme is essential for nicotine or (S)-6-hydroxynicotine degradation
-
-
?
additional information

?
-
-
transformation of 6-hydroxy-L-nicotine to 6-hydroxy-N-methylmyosmine, 6-hydroxypseudooxynicotine formation, overview
-
-
?
additional information
?
-
-
transformation of 6-hydroxy-L-nicotine to 6-hydroxy-N-methylmyosmine, 6-hydroxypseudooxynicotine formation, overview
-
-
?
additional information
?
-
-
enzyme production is induced by growing cells in D,L-nicotine as only source of carbon and nitrogen
-
-
?
additional information
?
-
-
enzyme production is induced by growing cells in D,L-nicotine as only source of carbon and nitrogen
-
-
?
additional information
?
-
-
enzyme production is induced by growing cells in D,L-nicotine as only source of carbon and nitrogen
-
-
?
additional information
?
-
-
it is synthesized only during the logarithmic and stationary phases of growth
-
-
?
additional information
?
-
-
no activity with 6-hydroxy-D-nicotine
-
-
?
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metabolism

-
pathways of nicotine degradation by bacteria
metabolism
-
the enzyme is involved in nicotine degradation, five hydroxylated-pyridine intermediates during the cell growth on nicotine and during transformation of nicotine within resting cells, overview. Agrobacterium strain S33 employs a novel pathway that is different from the two characterized pathways described in Arthrobacter and Pseudomonas. Agrobacterium strain S33 is able to transform nicotine to 6-hydroxypseudooxynicotine first via the pyridine pathway through 6-hydroxy-L-nicotine and 6-hydroxy-N-methylmyosmine, and then, it turns to the pyrrolidine pathway with the formation of 6-hydroxy-3-succinoylpyridine and 2,5-dihydroxypyridine. The cell extract can transform 6-hydroxypseudooxynicotine into 6-hydroxy-3-succinoylpyridine by coupling with 6-hydroxy-Lnicotine oxidation reaction by 6-hydroxy-L-nicotine oxidase. Pathways of nicotine degradation by bacteria,, overview
metabolism
the deletion and complementation of the nctB gene shows that this enzyme is essential for nicotine or (S)-6-hydroxynicotine degradation
metabolism
-
the enzyme catalyzes the oxidation of (S)-6-hydroxynicotine to 6-hydroxypseudooxynicotine during microbial catabolism of nicotine
metabolism
-
the enzyme is involved in nicotine degradation, five hydroxylated-pyridine intermediates during the cell growth on nicotine and during transformation of nicotine within resting cells, overview. Agrobacterium strain S33 employs a novel pathway that is different from the two characterized pathways described in Arthrobacter and Pseudomonas. Agrobacterium strain S33 is able to transform nicotine to 6-hydroxypseudooxynicotine first via the pyridine pathway through 6-hydroxy-L-nicotine and 6-hydroxy-N-methylmyosmine, and then, it turns to the pyrrolidine pathway with the formation of 6-hydroxy-3-succinoylpyridine and 2,5-dihydroxypyridine. The cell extract can transform 6-hydroxypseudooxynicotine into 6-hydroxy-3-succinoylpyridine by coupling with 6-hydroxy-Lnicotine oxidation reaction by 6-hydroxy-L-nicotine oxidase. Pathways of nicotine degradation by bacteria,, overview
-
physiological function

-
expression of the 6-hydroxy-L-nicotine oxidase gene allows the bacterium to take up L-nicotine
physiological function
-
expression of the 6-hydroxy-L-nicotine oxidase gene allows the bacterium to take up L-nicotine
-
additional information

the flavin may have a role in oxygen activation involving replacement of the water molecule by oxygen and superoxide formation. The orientation of the bound substrate relative to the isoalloxazine ring of the FAD cofactor is suitable for hydride transfer dehydrogenation at the carbon atom that forms the chiral center of the substrate molecule, substrate-binding mode, overview. In the dithionite-reduced 6HLNO, the natural substrate 6-hydroxy-L-nicotine is located in a tight cavity suggesting that the binding geometry of this unproductive complex may be closely similar as under oxidizing conditions
additional information
-
the flavin may have a role in oxygen activation involving replacement of the water molecule by oxygen and superoxide formation. The orientation of the bound substrate relative to the isoalloxazine ring of the FAD cofactor is suitable for hydride transfer dehydrogenation at the carbon atom that forms the chiral center of the substrate molecule, substrate-binding mode, overview. In the dithionite-reduced 6HLNO, the natural substrate 6-hydroxy-L-nicotine is located in a tight cavity suggesting that the binding geometry of this unproductive complex may be closely similar as under oxidizing conditions
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Schenk, S.; Hoelz, A.; Krauss, B.; Decker, K.
Gene structures and properties of enzymes of the plasmid-encoded nicotine catabolism of Arthrobacter nicotinovorans
J. Mol. Biol.
284
1323-1339
1998
Paenarthrobacter nicotinovorans
brenda
Grether-Beck, S.; Igloi, G.L.; Pust, S.; Schilz, E.; Decker, K.; Brandsch, R.
Structural analysis and molybdenum-dependent expression of the pAO1-encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans
Mol. Microbiol.
13
929-936
1994
Paenarthrobacter nicotinovorans
brenda
Pust, S.; Vervoort, J.; Decker, K.; Bacher, A.; Muller, F.
13C, 15N, and 31P NMR studies on 6-hydroxy-L-nicotine oxidase from Arthrobacter oxidans
Biochemistry
28
516-521
1989
Paenarthrobacter nicotinovorans
brenda
Brandsch, R.; Hinkkanen, A.E.; 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
Eur. J. Biochem.
167
315-320
1987
Paenarthrobacter nicotinovorans
brenda
Swafford, J.R.; Reeves, H.C.; Brandsch, R.
Localization of the enantiozymes of 6-hydroxy-nicotine oxidase in Arthrobacter oxidans by electron immunochemistry
J. Bacteriol.
163
792-795
1985
Paenarthrobacter nicotinovorans
brenda
Hinkkanen, A.; Lilius, E.M.; Nowack, J.; Maas, R.; Decker, K.
Purification of the flavoproteins 6-hydroxy-D- and 6-hydroxy-L-nicotine oxidase using hydrophobic affinity chromatography
Hoppe-Seyler's Z. Physiol. Chem.
364
801-806
1983
Paenarthrobacter nicotinovorans
brenda
Decker, K.; Dai, V.D.; Möhler, H.; Bruhmuller, M.
D- and L-6-hydroxynicotine oxidase, enantioenzymes of Arthrobacter oxidans
Z. Naturforsch. B
27
1072-1073
1972
Paenarthrobacter nicotinovorans
brenda
Palmer, G.; Massey, V.
Mechanisms of flavoprotein catalysis
Biol. Oxidations (Singer, T. P. , ed. )
263-300
1968
Paenarthrobacter nicotinovorans
-
brenda
Dai, V.D.; Decker, K.; Sund, H.
Purification and properties of L-6-hydroxynicotine oxidase
Eur. J. Biochem.
4
95-102
1968
Paenarthrobacter nicotinovorans
brenda
Decker, K.; Dai, V.D.
Mechanism and specifcity of L- and D-6-hydroxynicotine oxidase
Eur. J. Biochem.
3
132-138
1967
Paenarthrobacter nicotinovorans
brenda
Decker, K.; Bleeg, H.
Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxidans
Biochim. Biophys. Acta
105
313-324
1965
Paenarthrobacter nicotinovorans
brenda
Schenk, S.; Decker, K.
Horizontal gene transfer involved in the convergent evolution of the plasmid-encoded enantioselective 6-hydroxynicotine oxidases
J. Mol. Evol.
48
178-186
1999
Paenarthrobacter nicotinovorans
brenda
Ganas, P.; Brandsch, R.
Uptake of L-nicotine and of 6-hydroxy-L-nicotine by Arthrobacter nicotinovorans and by Escherichia coli is mediated by facilitated diffusion and not by passive diffusion or active transport
Microbiology
155
1866-1877
2009
Paenarthrobacter nicotinovorans, Paenarthrobacter nicotinovorans PAO1
brenda
Kachalova, G.S.; Bourenkov, G.P.; Mengesdorf, T.; Schenk, S.; Maun, H.R.; Burghammer, M.; Riekel, C.; Decker, K.; Bartunik, H.D.
Crystal structure analysis of free and substrate-bound 6-hydroxy-L-nicotine oxidase from Arthrobacter nicotinovorans
J. Mol. Biol.
396
785-799
2010
Paenarthrobacter nicotinovorans (Q93NH4), Paenarthrobacter nicotinovorans
brenda
Wang, S.; Huang, H.; Xie, K.; Xu, P.
Identification of nicotine biotransformation intermediates by Agrobacterium tumefaciens strain S33 suggests a novel nicotine degradation pathway
Appl. Microbiol. Biotechnol.
95
1567-1578
2012
Agrobacterium tumefaciens, Agrobacterium tumefaciens S33, Paenarthrobacter nicotinovorans
brenda
Kachalova, G.; Decker, K.; Holt, A.; Bartunik, H.D.
Crystallographic snapshots of the complete reaction cycle of nicotine degradation by an amine oxidase of the monoamine oxidase (MAO) family
Proc. Natl. Acad. Sci. USA
108
4800-4805
2011
Paenarthrobacter nicotinovorans
brenda
Qiu, J.; Wei, Y.; Ma, Y.; Wen, R.; Wen, Y.; Liu, W.
A novel (S)-6-hydroxynicotine oxidase gene from Shinella sp. strain HZN7
Appl. Environ. Microbiol.
80
5552-5560
2014
Shinella sp. (A0A075BSX9), Shinella sp.
brenda
Yu, H.; Tang, H.; Zhu, X.; Li, Y.; Xu, P.
Molecular mechanism of nicotine degradation by a newly isolated strain, Ochrobactrum sp. strain SJY1
Appl. Environ. Microbiol.
81
272-281
2015
Ochrobactrum sp. SJY1 (A0A075XFI8)
brenda
Fitzpatrick, P.F.; Chadegani, F.; Zhang, S.; Dougherty, V.
Mechanism of flavoprotein L-6-hydroxynicotine oxidase pH and solvent isotope effects and identification of key active site residues
Biochemistry
56
869-875
2017
Paenarthrobacter nicotinovorans
brenda