1.5.3.5: (S)-6-hydroxynicotine oxidase
This is an abbreviated version!
For detailed information about (S)-6-hydroxynicotine oxidase, go to the full flat file.
Word Map on EC 1.5.3.5
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1.5.3.5
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arthrobacter
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6-hydroxy-d-nicotine
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nicotinovorans
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oxidans
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flavin
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fad
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flavoenzyme
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nicotine-degrading
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monoamine
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flavoproteins
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hydride
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6-hydroxypseudooxynicotine
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dehydrogenation
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pseudooxynicotine
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d-specific
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pyrrolidine
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dithionite-reduced
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carbon-carbon
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self-formed
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fad-binding
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s-nicotine
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l-enantiomer
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fitzpatrick
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carbon-nitrogen
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isoalloxazine
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6-hdno
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substrate-reduced
- 1.5.3.5
- arthrobacter
- 6-hydroxy-d-nicotine
- nicotinovorans
- oxidans
- flavin
- fad
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flavoenzyme
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nicotine-degrading
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monoamine
- flavoproteins
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hydride
- 6-hydroxypseudooxynicotine
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dehydrogenation
- pseudooxynicotine
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d-specific
- pyrrolidine
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dithionite-reduced
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carbon-carbon
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self-formed
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fad-binding
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s-nicotine
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l-enantiomer
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fitzpatrick
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carbon-nitrogen
- isoalloxazine
- 6-hdno
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substrate-reduced
Reaction
Synonyms
6-HLNO, 6-hydroxy-L-nicotine oxidase, 6-hydroxy-L-nicotine:oxygen oxidoreductase, 6HLNO, flavoprotein nicotine oxidoreductase, L-6-hydroxynicotine oxidase, LHNO, MAO, NdpB, NicA2, NOX, VppB
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General Information
General Information on EC 1.5.3.5 - (S)-6-hydroxynicotine oxidase
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evolution
metabolism
physiological function
additional information
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enzyme is part of a nicotine-degrading gene cluster, ndp, containing the nicotine hydroxylase, 6-hydroxy-L-nicotine oxidase, 6-hydroxypseudooxynicotine oxidase, and 6-hydroxy-3-succinyl-pyridine monooxygenase responsible for catalyzing the transformation of nicotine to 2,5-dihydropyridine. The linked ndpHFEG genes shared by the variant of the pyridine and pyrrolidine pathways and pyrrolidine pathways indicate that these two pathways might share the same origin
evolution
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enzyme is part of a nicotine-degrading gene cluster, ndp, containing the nicotine hydroxylase, 6-hydroxy-L-nicotine oxidase, 6-hydroxypseudooxynicotine oxidase, and 6-hydroxy-3-succinyl-pyridine monooxygenase responsible for catalyzing the transformation of nicotine to 2,5-dihydropyridine. The linked ndpHFEG genes shared by the variant of the pyridine and pyrrolidine pathways and pyrrolidine pathways indicate that these two pathways might share the same origin
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metabolism
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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
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the enzyme catalyzes the oxidation of (S)-6-hydroxynicotine to 6-hydroxypseudooxynicotine during microbial catabolism of nicotine
metabolism
resiudes Asn166, Tyr311, and Lys287 as well as an active site water molecule have roles in the catalysis of the enzyme. A hydride transfer mechanism is the only viable mechanism for catalysis. During the hydride transfer process an active site water molecule bridges FAD and Lys287 through H-bonding interaction. A series of H-bonding interactions coupled with van der Waals interactions keep FAD and substrate S-6-hydroxynicotine closer. FAD achieves a bent conformation
metabolism
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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
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expression of the 6-hydroxy-L-nicotine oxidase gene allows the bacterium to take up L-nicotine
physiological function
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after disruption of ndpB gene, the mutant strain loses the ability to grow on nicotine and accumulates 6-hydroxynicotine
physiological function
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after disruption of ndpB gene, the mutant strain loses the ability to grow on nicotine and accumulates 6-hydroxynicotine
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physiological function
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expression of the 6-hydroxy-L-nicotine oxidase gene allows the bacterium to take up L-nicotine
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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
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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