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
ECTree
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Engineering
Engineering on EC 1.5.3.5 - (S)-6-hydroxynicotine oxidase
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D166Q
mutation slightly reduces the KM for nicotine, it also reduced enzyme turnover by 5fold with nicotine
K287M
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mutation results in an about 10-fold decreases in kcat/Km and k(red) for (S)-6-hydroxynicotine and a 6000-fold decrease in the kcat/Km value for oxygen
N166A
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mutation results in an about 30fold decrease in kcat/Km and k(red) for (S)-6-hydroxynicotine, respectively, with larger effects on the kcat/Km value for (S)-6-hydroxynornicotine. The shapes of the pH profiles are not altered
R274A/Y311W/C417W
combination of mutations predicted to enhance enzyme stability, and mutation Y311W. The triple mutant displays an increased kcat value for nicotine resulting in a comparatively robust oxidation of (S)-nicotine, at the same time reducing the specificity for (S)-OH-nicotine by more than 100fold and increasing that for (S)-nicotine by more than fold
Y311F
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mutation results in an about 30fold decrease in kcat/Km and k(red) for (S)-6-hydroxynicotine, respectively, with larger effects on the kcat/Km value for (S)-6-hydroxynornicotine. The shapes of the pH profiles are not altered
Y311W
active site residue Tyr311 forms a hydrogen bond with the hydroxyl group of (S)-6-OH-nicotine within the catalytic pocket. Replacement by a tryptophan residue reduces the kcat for (S)-6-OH-nicotine by more than 6fold
N462H
the variant shows moderately higher oxidase activity, reductive half-reaction using (S)-nicotine is significantly slower than that of wild-type enzyme
W427V
the variant shows moderately higher oxidase activity, reductive half-reaction using (S)-nicotine is significantly slower than that of wild-type enzyme
N462H
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the variant shows moderately higher oxidase activity, reductive half-reaction using (S)-nicotine is significantly slower than that of wild-type enzyme
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W427V
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the variant shows moderately higher oxidase activity, reductive half-reaction using (S)-nicotine is significantly slower than that of wild-type enzyme
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additional information
adding a maltose-binding protein tag onto the N-terminus markedly increases the thermal stability of the enzyme and increases the observed Vmax value for 6-OH-nicotine by about 4.5fold, due to an increase in the occupancy of the flavin cofactor following expression and purification
additional information
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adding a maltose-binding protein tag onto the N-terminus markedly increases the thermal stability of the enzyme and increases the observed Vmax value for 6-OH-nicotine by about 4.5fold, due to an increase in the occupancy of the flavin cofactor following expression and purification