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Information on EC 1.5.3.5 - (S)-6-hydroxynicotine oxidase for references in articles please use BRENDA:EC1.5.3.5
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EC Tree
IUBMB 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).
The enzyme appears in viruses and cellular organisms
Synonyms
6-hydroxy-L-nicotine oxidase, 6-hydroxy-L-nicotine:oxygen oxidoreductase, 6HLNO, L-6-hydroxynicotine oxidase, LHNO, MAO, VppB,
more
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6-hydroxy-L-nicotine oxidase
6-hydroxy-L-nicotine:oxygen oxidoreductase
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L-6-hydroxynicotine oxidase
6-hydroxy-L-nicotine oxidase
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6-hydroxy-L-nicotine oxidase
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6-hydroxy-L-nicotine oxidase
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6-hydroxy-L-nicotine oxidase
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6-hydroxy-L-nicotine oxidase
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6-hydroxy-L-nicotine oxidase
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6-hydroxy-L-nicotine oxidase
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6HLNO
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L-6-hydroxynicotine oxidase
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L-6-hydroxynicotine oxidase
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(S)-6-hydroxynicotine + H2O + O2 = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
(S)-6-hydroxynicotine + O2 = 5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol + H2O2
(1a)
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5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol + H2O = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one
(1b), spontaneous
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(S)-6-hydroxynicotine + H2O + O2 = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
overall reaction
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(S)-6-hydroxynicotine + H2O + O2 = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
mechanism and roles of active site residues: Asn166 and Tyr311 bind the substrate, while Lys287 forms a water-mediated hydrogen bond with flavin N5
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(S)-6-hydroxynicotine:oxygen oxidoreductase
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).
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(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
?
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(S)-nicotine + H2O + O2
N-methylmyosmine + H2O2
the enzyme converts (S)-nicotine into N-methylmyosmine, which spontaneously hydrolyzes into pseudooxynicotine
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?
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
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6-hydroxy-L-nicotine + H2O + O2
6-hydroxy-N-methylmyosmine + NH3 + H2O2
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?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
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?
L-6-hydroxy-nor-nicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-aminobutan-1-one + H2O2
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additional information
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(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
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(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
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(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
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?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
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?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
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?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
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?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
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?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
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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
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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
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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
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transitional product is 6-hydroxy-N-methylmyosmine that hydrolyses spontaneously
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
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(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
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?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
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(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
the enzyme is involved in degradation of nicotine
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(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
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(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
absolute stereospecificity on the L-form
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(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
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(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
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the enzyme catalyzes the oxidation of (S)-6-hydroxynicotine to 6-hydroxypseudooxynicotine during microbial catabolism of nicotine
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(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
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(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
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(S)-6-hydroxynicotine + H2O + O2
6-hydroxy-pseudooxynicotine + H2O2
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(S)-6-hydroxynicotine + H2O + O2
6-hydroxy-pseudooxynicotine + H2O2
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additional information
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transformation of 6-hydroxy-L-nicotine to 6-hydroxy-N-methylmyosmine, 6-hydroxypseudooxynicotine formation, overview
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additional information
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measurement of enzyme activity using dichlorindophenol. 6-Hydroxypseudooxynicotine forms from 6-hydroxy-N-methylmyosmine non-enzymatically
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additional information
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transformation of 6-hydroxy-L-nicotine to 6-hydroxy-N-methylmyosmine, 6-hydroxypseudooxynicotine formation, overview
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additional information
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measurement of enzyme activity using dichlorindophenol. 6-Hydroxypseudooxynicotine forms from 6-hydroxy-N-methylmyosmine non-enzymatically
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additional information
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also oxidizes circular secondary and tertiary amines
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additional information
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enzyme production is induced by growing cells in D,L-nicotine as only source of carbon and nitrogen
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additional information
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enzyme production is induced by growing cells in D,L-nicotine as only source of carbon and nitrogen
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additional information
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enzyme production is induced by growing cells in D,L-nicotine as only source of carbon and nitrogen
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additional information
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it is synthesized only during the logarithmic and stationary phases of growth
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additional information
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no activity with 6-hydroxy-D-nicotine
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additional information
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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
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additional information
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(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
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?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
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(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
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?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
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(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
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(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
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(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
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?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
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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
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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
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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
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transitional product is 6-hydroxy-N-methylmyosmine that hydrolyses spontaneously
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
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(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
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(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
the enzyme is involved in degradation of nicotine
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(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
absolute stereospecificity on the L-form
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?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
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the enzyme catalyzes the oxidation of (S)-6-hydroxynicotine to 6-hydroxypseudooxynicotine during microbial catabolism of nicotine
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(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
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additional information
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transformation of 6-hydroxy-L-nicotine to 6-hydroxy-N-methylmyosmine, 6-hydroxypseudooxynicotine formation, overview
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additional information
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transformation of 6-hydroxy-L-nicotine to 6-hydroxy-N-methylmyosmine, 6-hydroxypseudooxynicotine formation, overview
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additional information
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enzyme production is induced by growing cells in D,L-nicotine as only source of carbon and nitrogen
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additional information
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enzyme production is induced by growing cells in D,L-nicotine as only source of carbon and nitrogen
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additional information
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enzyme production is induced by growing cells in D,L-nicotine as only source of carbon and nitrogen
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additional information
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it is synthesized only during the logarithmic and stationary phases of growth
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additional information
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no activity with 6-hydroxy-D-nicotine
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
FAD
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1 FAD per subunit, non-covalently bound
FAD
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1 FAD per subunit, non-covalently bound; has an adenylate-binding domain
FAD
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1 FAD per subunit, non-covalently bound; 4 mol FAD per mol protein
FAD
binding domain structure, overview. The flavin may have a role in oxygen activation involving replacement of the water molecule by oxygen and superoxide formation
FAD
flavoprotein. FAD content is determined to be 1.0 of FAD per mole subunit
FAD
tightly bound to the enzyme
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additional information
the reaction progresses without the participation of metal ions
additional information
the enzyme does not require Al3+, Ca2+, Mg2+, or Mn2+ for its activity
additional information
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the enzyme does not require Al3+, Ca2+, Mg2+, or Mn2+ for its activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ag+
1 mM, about 85% inhibition
Co2+
1 mM, about 10% inhibition
Cu2+
1 mM, about 85% inhibition
EDTA
incubation for 1 h completely inhibits enzymatic activity
Hg2+
1 mM, about 80% inhibition
HgCl2
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100% inhibition at 0.005 mM
methylene blue
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strong inhibitor
Na2MoO4
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12% inhibition at 0.05 mM
o-phenanthroline
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69% inhibition at 9 mM
p-chloromercuriphenylsulfonate
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60% inhibition at 0.025 mM, inhibition can be reversed by an excess of thiol compounds
SDS
incubation for 1 h completely inhibits enzymatic activity
Urea
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at 4 M, 38% inhibition and at 7.2 M, 93% inhibition
Zn2+
1 mM, about 25% inhibition
ZnSO4
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57% inhibition at 0.05 mM
6-hydroxy-D-nicotine
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competitive inhibitor
6-hydroxy-D-nicotine
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50% inhibition at 0.18 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MoO42-
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induces enzyme expression activity
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0.011 - 24.6
(S)-6-hydroxynicotine
0.064 - 1.2
(S)-6-hydroxynornicotine
0.396
(S)-nicotine
pH 7.0, 40°C
0.02
6-hydroxy-L-nicotine
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0.011
(S)-6-hydroxynicotine
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pH 7.0, 25°C, mutant enzyme K287M
0.019
(S)-6-hydroxynicotine
pH 7.0, 40°C
0.02
(S)-6-hydroxynicotine
pH and temperature not specified in the publication
0.13
(S)-6-hydroxynicotine
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pH 7.0, 25°C, wild-type enzyme
0.2
(S)-6-hydroxynicotine
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pH 7.0, 25°C, mutant enzyme Y311F
0.34
(S)-6-hydroxynicotine
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pH 7.0, 25°C, mutant enzyme N166A
24.6
(S)-6-hydroxynicotine
pH 8.0, 25°C
0.064
(S)-6-hydroxynornicotine
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pH 7.0, 25°C, wild-type enzyme
1.1
(S)-6-hydroxynornicotine
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pH 7.0, 25°C, mutant enzyme Y311F
1.2
(S)-6-hydroxynornicotine
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pH 7.0, 25°C, mutant enzyme N166A
0.19
O2
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pH 7.0, 25°C, mutant enzyme Y311F, cosubstrate: (S)-6-hydroxynicotine
0.2
O2
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pH 7.0, 25°C, mutant enzyme N166A, cosubstrate: (S)-6-hydroxynicotine
0.29
O2
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pH 7.0, 25°C, wild-type enzyme, cosubstrate: (S)-6-hydroxynicotine
0.46
O2
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pH 7.0, 25°C, wild-type enzyme, cosubstrate: (S)-6-hydroxynornicotine
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0.26 - 78
(S)-6-hydroxynicotine
2.5 - 16
(S)-6-hydroxynornicotine
2.03
(S)-nicotine
pH 7.0, 40°C
29.3
6-hydroxy-L-nicotine
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0.26
(S)-6-hydroxynicotine
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pH 7.0, 25°C, mutant enzyme K287M
4.8
(S)-6-hydroxynicotine
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pH 7.0, 25°C, mutant enzyme N166A
7.3
(S)-6-hydroxynicotine
pH 7.0, 40°C
20.9
(S)-6-hydroxynicotine
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pH 7.0, 25°C, mutant enzyme Y311F
25.8
(S)-6-hydroxynicotine
pH 8.0, 25°C
78
(S)-6-hydroxynicotine
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pH 7.0, 25°C, wild-type enzyme
2.5
(S)-6-hydroxynornicotine
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pH 7.0, 25°C, mutant enzyme N166A
9.1
(S)-6-hydroxynornicotine
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pH 7.0, 25°C, mutant enzyme Y311F
16
(S)-6-hydroxynornicotine
-
pH 7.0, 25°C, wild-type enzyme
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14 - 600
(S)-6-hydroxynicotine
2 - 370
(S)-6-hydroxynornicotine
0.195
(S)-nicotine
pH 7.0, 40°C
14
(S)-6-hydroxynicotine
-
pH 7.0, 25°C, mutant enzyme N166A
24
(S)-6-hydroxynicotine
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pH 7.0, 25°C, mutant enzyme K287M
103
(S)-6-hydroxynicotine
-
pH 7.0, 25°C, mutant enzyme Y311F
379
(S)-6-hydroxynicotine
pH 7.0, 40°C
600
(S)-6-hydroxynicotine
-
pH 7.0, 25°C, wild-type enzyme
2
(S)-6-hydroxynornicotine
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pH 7.0, 25°C, mutant enzyme N166A
8.6
(S)-6-hydroxynornicotine
-
pH 7.0, 25°C, mutant enzyme Y311F
370
(S)-6-hydroxynornicotine
-
pH 7.0, 25°C, wild-type enzyme
0.048
O2
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pH 7.0, 25°C, mutant enzyme K287M, cosubstrate: (S)-6-hydroxynicotine
24
O2
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pH 7.0, 25°C, mutant enzyme N166A, cosubstrate: (S)-6-hydroxynicotine
110
O2
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pH 7.0, 25°C, mutant enzyme Y311F, cosubstrate: (S)-6-hydroxynicotine
150
O2
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pH 7.0, 25°C, wild-type enzyme, cosubstrate: (S)-6-hydroxynornicotine
270
O2
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pH 7.0, 25°C, wild-type enzyme, cosubstrate: (S)-6-hydroxynicotine
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.1
(R)-6-hydroxynicotine
pH and temperature not specified in the publication
0.1
6-hydroxy-D-nicotine
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0.31
DL-2-hydroxynicotine
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0.462
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strain S33, pH 7.0, 30°C
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7 - 7.5
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assay at
8
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7 - 9
pH 7.0: about 65% of maximal activity, pH 9.0: about 25% of maximal activity
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30
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assay at
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15 - 65
15°C: about 40% of maximal activity, 65°C: about 55% of maximal activity
20 - 50
20°C: about 65% of maximal activity, 50°C: about 70% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
isolated from tobacco plant rhizosphere in Shandong Province, China
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brenda
isolated from tobacco plant rhizosphere in Shandong Province, China
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UniProt
brenda
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brenda
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UniProt
brenda
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brenda
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UniProt
brenda
formerly Arthrobacter oxidans
392430 , 392431 , 392432 , 392433 , 392434 , 392435 , 392436 , 392437 , 392438 , 392439 , 392440 , 392441
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brenda
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brenda
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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
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pathways of nicotine degradation by bacteria
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
-
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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physiological function
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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
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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
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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C1B574_RHOOB
Rhodococcus opacus (strain B4)
418
0
44865
TrEMBL
O86101_PAENI
425
0
46277
TrEMBL
O86101_PAENI
425
0
46277
TrEMBL
A0A075BSX9_9RHIZ
437
0
48736
TrEMBL
Q93NH4_PAENI
425
0
46335
TrEMBL
A0A075XFI8_9RHIZ
437
0
48736
TrEMBL
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46265
-
2 * 46265, amino acid analysis
47000
-
2 * 47000, sedimentation equilibrium
93000
-
sedimentation equilibrium
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dimer
the active enzyme exists as a stable dimer in solution
homodimer
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2 * 46265, amino acid analysis
homodimer
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2 * 47000, sedimentation equilibrium
homodimer
2 * 50000, SDS-PAGE
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lipoprotein
a diacylglycerophospholipid molecule is non-covalently bound to each enzyme protomer. The fatty acid chains occupy hydrophobic channels that penetrate deep into the interior of the substrate-binding domain of each subunit. The solvent-exposed glycerophosphate moiety is located at the subunit-subunit interface
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forms hexagonal crystals in ammonium sulfate solution
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His-tagged and untagged free enzyme and complex of dithionite-reduced 6HLNO with the natural substrate 6-hydroxy-L-nicotine X-ray diffraction structure determination and analysis at 1.95 A and 2.05 A resolution, respectively, combined isomorphous/multiple-wavelength anomalous dispersion phasing; to 1.95 A resolution. A diacylglycerophospholipid molecule is non-covalently bound to each protomer of 6HLNO. The fatty acid chains occupy hydrophobic channels that penetrate deep into the interior of the substrate-binding domain of each subunit. The solvent-exposed glycerophosphate moiety is located at the subunit-subunit interface. In the crystal structure of a complex of dithionite-reduced 6HLNO with the natural substrate 6-hydroxy-L-nicotine at 2.05 A resolution, the location of the substrate in a tight cavity suggests that the binding geometry of this unproductive complex may be closely similar as under oxidizing conditions. A comparison of the substrate-binding modes of 6HLNO and 6-hydroxy-D-nicotine oxidase, EC 1.5.3.6, based on models of complexes with the D-substrate, suggests that the two enzymes orient the enantiomeric substrates in mirror symmetry with respect to the plane of the flavin
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K287M
-
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
Y311F
-
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
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10
40°C, 1 h, about 30% loss of activity
741686
6 - 9
-
very unstable under pH 6
392438
7 - 8
40°C, 1 h, no loss of activity
741686
5
-
very unstable below pH 5
392439
5
40°C, 1 h, about 50% loss of activity
741686
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40
-
75% activity after 15 min
5 - 40
1 h, no loss of activity
50
-
9% activity after 5 min
50
1 h, about 15% loss of activity
60
-
2% activity after 5 min
60
1 h, about 65% loss of activity
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0°C, saturated ammonium sulfate solution, 2 weeks, little inactivation
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expressed in Escherichia coli JM105
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expressed in Escherichia coli JM109
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expressed in Escherichia coli K12 strain HB101
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expressed in Escherichia coli XL10-Gold cells
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expression in Escherichi coli
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expression in Escherichia coli
expression in Escherichia coli BL21(DE3)
overexpressed in Escherichia coli BL21(DE3) as a C-terminal His6-tagged fusion protein
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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, Paenarthrobacter nicotinovorans (Q93NH4)
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
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