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Information on EC 1.5.3.5 - (S)-6-hydroxynicotine oxidase
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1.5.3.5 (S)-6-hydroxynicotine oxidaseIUBMB 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).
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Word Map
- 1.5.3.5
- arthrobacter
- 6-hydroxy-d-nicotine
- nicotinovorans
- oxidans
- flavin
- fad
-
flavoenzyme
-
nicotine-degrading
- flavoproteins
-
monoamine
- pseudooxynicotine
-
dehydrogenation
- 6-hydroxypseudooxynicotine
- pyrrolidine
-
d-specific
-
fitzpatrick
-
s-nicotine
-
fad-binding
-
dithionite-reduced
- isoalloxazine
-
l-enantiomer
-
self-formed
-
substrate-reduced
- 6-hdno
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
6-hydroxy-L-nicotine oxidase, 6-hydroxy-L-nicotine:oxygen oxidoreductase, 6HLNO, L-6-hydroxynicotine oxidase, LHNO, MAO, VppB, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6-hydroxy-L-nicotine oxidase
6HLNO
L-6-hydroxynicotine oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-6-hydroxynicotine + H2O + O2 = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
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
-
-
(S)-6-hydroxynicotine + H2O + O2 = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
overall reaction
-
-
(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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(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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CAS REGISTRY NUMBER
COMMENTARY
37256-29-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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)-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
-
-
-
-
?
L-6-hydroxy-nor-nicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-aminobutan-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
-
-
-
?
(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-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
-
-
-
?
(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
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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
-
-
-
-
?
(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
-
-
-
?
(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-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
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
1 FAD per subunit, non-covalently bound
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
-
the enzyme does not require Al3+, Ca2+, Mg2+, or Mn2+ for its activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-chloromercuriphenylsulfonate
-
60% inhibition at 0.025 mM, inhibition can be reversed by an excess of thiol compounds
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.011
(S)-6-hydroxynicotine
-
pH 7.0, 25°C, mutant enzyme K287M
0.02
(S)-6-hydroxynicotine
pH and temperature not specified in the publication
0.2
(S)-6-hydroxynicotine
-
pH 7.0, 25°C, mutant enzyme Y311F
0.34
(S)-6-hydroxynicotine
-
pH 7.0, 25°C, mutant enzyme N166A
0.064
(S)-6-hydroxynornicotine
-
pH 7.0, 25°C, wild-type enzyme
1.1
(S)-6-hydroxynornicotine
-
pH 7.0, 25°C, mutant enzyme Y311F
1.2
(S)-6-hydroxynornicotine
-
pH 7.0, 25°C, mutant enzyme N166A
0.19
O2
-
pH 7.0, 25°C, mutant enzyme Y311F, cosubstrate: (S)-6-hydroxynicotine
0.2
O2
-
pH 7.0, 25°C, mutant enzyme N166A, cosubstrate: (S)-6-hydroxynicotine
0.29
O2
-
pH 7.0, 25°C, wild-type enzyme, cosubstrate: (S)-6-hydroxynicotine
0.46
O2
-
pH 7.0, 25°C, wild-type enzyme, cosubstrate: (S)-6-hydroxynornicotine
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.26
(S)-6-hydroxynicotine
-
pH 7.0, 25°C, mutant enzyme K287M
4.8
(S)-6-hydroxynicotine
-
pH 7.0, 25°C, mutant enzyme N166A
20.9
(S)-6-hydroxynicotine
-
pH 7.0, 25°C, mutant enzyme Y311F
2.5
(S)-6-hydroxynornicotine
-
pH 7.0, 25°C, mutant enzyme N166A
9.1
(S)-6-hydroxynornicotine
-
pH 7.0, 25°C, mutant enzyme Y311F
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
103
(S)-6-hydroxynicotine
-
pH 7.0, 25°C, mutant enzyme Y311F
2
(S)-6-hydroxynornicotine
-
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
-
pH 7.0, 25°C, mutant enzyme K287M, cosubstrate: (S)-6-hydroxynicotine
24
O2
-
pH 7.0, 25°C, mutant enzyme N166A, cosubstrate: (S)-6-hydroxynicotine
110
O2
-
pH 7.0, 25°C, mutant enzyme Y311F, cosubstrate: (S)-6-hydroxynicotine
150
O2
-
pH 7.0, 25°C, wild-type enzyme, cosubstrate: (S)-6-hydroxynornicotine
270
O2
-
pH 7.0, 25°C, wild-type enzyme, cosubstrate: (S)-6-hydroxynicotine
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
(R)-6-hydroxynicotine
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
pH 7.0: about 65% of maximal activity, pH 9.0: about 25% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from tobacco plant rhizosphere in Shandong Province, China
-
-
brenda
isolated from tobacco plant rhizosphere in Shandong Province, China
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
the active enzyme exists as a stable dimer in solution
homodimer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
60
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, saturated ammonium sulfate solution, 2 weeks, little inactivation
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpressed in Escherichia coli BL21(DE3) as a C-terminal His6-tagged fusion protein
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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, Paenarthrobacter nicotinovorans, Agrobacterium tumefaciens S33
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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