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Enzyme Nomenclature
Information on EC 1.5.99.4 - nicotine dehydrogenase
Word Map on EC 1.5.99.4
- 1.5.99.4
- arthrobacter
- barkeri
- molybdopterins
-
clostridium
- xanthine
- molybdenum
-
selenium-containing
-
nicotinovorans
- 6-hydroxynicotine
- 6-hydroxy-l-nicotine
- fad
- selenide
- selenocysteine
-
selenoproteins
-
organoselenium
-
acid-labile
-
hydroxylases
- pyrrolidine
- tungsten
-
selenium-dependent
-
molybdenum-containing
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mo-containing
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.5.99.4
-
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RECOMMENDED NAME
GeneOntology No.
nicotine dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-nicotine + acceptor + H2O = (S)-6-hydroxynicotine + reduced acceptor
; A metalloprotein (FMN). Acts on both (R)- and (S)-isomers
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
nicotine:acceptor 6-oxidoreductase (hydroxylating)
A metalloprotein (FMN). The enzyme can act on both the naturally found (S)-enantiomer and the synthetic (R)-enantiomer of nicotine, with retention of configuration in both cases [4].
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CAS REGISTRY NUMBER
COMMENTARY
37256-31-8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
30 kDa; strain bearing the catabolic plasmid pAO1, 2 stereospecific isozymes, gene 6hdno encodes the D-nicotine inducible and specific isozyme, gene 6hlno encodes the L-nicotine inducible and specific isozyme
SwissProt
30 kDa; strain bearing the catabolic plasmid pAO1, gene 6hdno encodes the D-nicotine inducible and specific isozyme
SwissProt
87.7 kDa; strain bearing the catabolic plasmid pAO1, 2 stereospecific isozymes, gene 6hdno encodes the D-nicotine inducible and specific isozyme, gene 6hlno encodes the L-nicotine inducible and specific isozyme
SwissProt
87.7 kDa; strain bearing the catabolic plasmid pAO1, gene 6hdno encodes the D-nicotine inducible and specific isozyme
SwissProt
small 17.8 kDa subunit; strain bearing the catabolic plasmid pAO1, 2 stereospecific isozymes, gene 6hdno encodes the D-nicotine inducible and specific isozyme, gene 6hlno encodes the L-nicotine inducible and specific isozyme
SwissProt
small 17.8 kDa subunit; strain bearing the catabolic plasmid pAO1, gene 6hdno encodes the D-nicotine inducible and specific isozyme
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
a nox disruption mutant of strain HZN6 loses the ability to degrade nicotine, but not pseudooxynicotine
malfunction
-
a nox disruption mutant of strain HZN6 loses the ability to degrade nicotine, but not pseudooxynicotine
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metabolism
the enzyme is responsible for the first step of nicotine degradation
metabolism
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the enzyme is responsible for the first step of nicotine degradation
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physiological function
the enzyme nonenantioselectively degrades nicotine to pseudooxynicotine
physiological function
-
the enzyme nonenantioselectively degrades nicotine to pseudooxynicotine
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additional information
the conserved FAD-binding GXGXXG motif and His456 are essential for nicotine degradation activity
additional information
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the conserved FAD-binding GXGXXG motif and His456 are essential for nicotine degradation activity
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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
(R)-nicotine + acceptor + H2O
(R)-6-hydroxynicotine + reduced acceptor
-
-
-
?
(S)-nicotine + acceptor + H2O
(S)-nicotine delta1',5'-iminium ion + reduced acceptor
-
-
-
?
(S)-nicotine + acceptor + H2O
nicotine-N-oxide + reduced acceptor
-
-
-
?
(S)-nicotine + acceptor + H2O
nornicotine + reduced acceptor
-
-
-
?
anabasine + acceptor + H2O
6-hydroxyanabasine + reduced acceptor
-
-
-
?
D-nicotine + acceptor + H2O
(R)-6-hydroxynicotine + reduced acceptor
isozyme specific for the D-isomer
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-
?
DL-nicotine + ?
6-hydroxynicotine + ?
-
first enzyme in nicotine pathway
-
?
nicotine-N-oxide + acceptor + H2O
6-hydroxynicotine-N-oxide + reduced acceptor
-
-
-
?
nornicotine + acceptor + H2O
6-hydroxynornicotine + reduced acceptor
-
-
-
?
(RS)-nicotine + acceptor + H2O
pseudooxynicotine + reduced acceptor
via N-methylmyosmine, which then spontaneously hydrolyzes to pseudooxynicotine. The two enantiomers are degraded at approximately the same rate, indicating that NOX does not show chiral selectivity
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-
?
(RS)-nicotine + acceptor + H2O
pseudooxynicotine + reduced acceptor
via N-methylmyosmine, which then spontaneously hydrolyzes to pseudooxynicotine. The two enantiomers are degraded at approximately the same rate, indicating that NOX does not show chiral selectivity
-
-
?
(S)-nicotine + acceptor + H2O
pseudooxynicotine + reduced acceptor
via N-methylmyosmine, which then spontaneously hydrolyzes to pseudooxynicotine. The two enantiomers are degraded at approximately the same rate, indicating that NOX does not show chiral selectivity
-
-
?
(S)-nicotine + acceptor + H2O
pseudooxynicotine + reduced acceptor
via N-methylmyosmine, which then spontaneously hydrolyzes to pseudooxynicotine. The two enantiomers are degraded at approximately the same rate, indicating that NOX does not show chiral selectivity
-
-
?
L-nicotine + acceptor + H2O
(S)-6-hydroxynicotine + reduced acceptor
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-
-
-
?
L-nicotine + acceptor + H2O
(S)-6-hydroxynicotine + reduced acceptor
-
-
-
-
?
L-nicotine + acceptor + H2O
(S)-6-hydroxynicotine + reduced acceptor
-
-
-
-
?
L-nicotine + acceptor + H2O
(S)-6-hydroxynicotine + reduced acceptor
isozyme strictly specific for the L-isomer
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-
?
nicotine + acceptor + H2O
6-hydroxynicotine + reduced acceptor
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non-stereospecific enzyme if grown on L-nicotine, assayed with 2,6-dichlorophenolindophenol
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?
nicotine + acceptor + H2O
6-hydroxynicotine + reduced acceptor
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brilliant cresyl blue, methylene blue, 5-hydroxy-1,4-naphthoquinone, 2,6-dichlorophenolindophenol, menadione and vitamin K5 used as electron acceptors
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?
nicotine + acceptor + H2O
6-hydroxynicotine + reduced acceptor
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preferentially 2,6-dichlorophenolindophenol used as electron acceptor
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?
nicotine + acceptor + H2O
6-hydroxynicotine + reduced acceptor
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molybdate is required
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?
nicotine + acceptor + H2O
6-hydroxynicotine + reduced acceptor
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molybdate is required
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?
nicotine + acceptor + H2O
6-hydroxynicotine + reduced acceptor
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first enzyme in the nicotine degradation pathway
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?
nicotine + acceptor + H2O
6-hydroxynicotine + reduced acceptor
-
first enzyme in the nicotine degradation pathway
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?
nicotine + acceptor + H2O
6-hydroxynicotine + reduced acceptor
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-
-
?
nicotinic acid + acceptor + H2O
6-hydroxynicotinic acid + reduced acceptor
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-
-
?
nicotinic acid + acceptor + H2O
6-hydroxynicotinic acid + reduced acceptor
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cytochrome-linked oxidation, hydroxylation
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?
nicotinic acid + acceptor + H2O
6-hydroxynicotinic acid + reduced acceptor
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cytochrome-linked oxidation, hydroxylation
-
?
nicotinic acid + acceptor + H2O
6-hydroxynicotinic acid + reduced acceptor
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2,6-dichlorophenolindophenol used as electron acceptor
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?
nicotinic acid + acceptor + H2O
6-hydroxynicotinic acid + reduced acceptor
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2,6-dichlorophenolindophenol used as electron acceptor
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?
additional information
?
-
enzyme expression and activity is regulated by substrate and product level via transcription repressor HdnoR
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-
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additional information
?
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enzyme expression and activity is regulated by substrate and product level via transcription repressor HdnoR
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-
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additional information
?
-
enzyme expression and activity is regulated by substrate and product level via transcription repressor HdnoR
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additional information
?
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organism can grow on L-nicotine since it is converted to D-nicotine by a racemase
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additional information
?
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organism can grow on L-nicotine since it is converted to D-nicotine by a racemase
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-
-
additional information
?
-
organism can grow on L-nicotine since it is converted to D-nicotine by a racemase
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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
(R)-nicotine + acceptor + H2O
(R)-6-hydroxynicotine + reduced acceptor
Q59127, Q59128, Q59129
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-
-
?
D-nicotine + acceptor + H2O
(R)-6-hydroxynicotine + reduced acceptor
Q59127, Q59128, Q59129
isozyme specific for the D-isomer
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-
?
DL-nicotine + ?
6-hydroxynicotine + ?
-
first enzyme in nicotine pathway
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?
L-nicotine + acceptor + H2O
(S)-6-hydroxynicotine + reduced acceptor
Q59127, Q59128, Q59129
isozyme strictly specific for the L-isomer
-
-
?
(S)-nicotine + acceptor + H2O
pseudooxynicotine + reduced acceptor
M4T5L3
via N-methylmyosmine, which then spontaneously hydrolyzes to pseudooxynicotine. The two enantiomers are degraded at approximately the same rate, indicating that NOX does not show chiral selectivity
-
-
?
(S)-nicotine + acceptor + H2O
pseudooxynicotine + reduced acceptor
M4T5L3
via N-methylmyosmine, which then spontaneously hydrolyzes to pseudooxynicotine. The two enantiomers are degraded at approximately the same rate, indicating that NOX does not show chiral selectivity
-
-
?
nicotine + acceptor + H2O
6-hydroxynicotine + reduced acceptor
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first enzyme in the nicotine degradation pathway
-
?
nicotine + acceptor + H2O
6-hydroxynicotine + reduced acceptor
-
first enzyme in the nicotine degradation pathway
-
?
additional information
?
-
Q59127
enzyme expression and activity is regulated by substrate and product level via transcription repressor HdnoR
-
-
-
additional information
?
-
Q59128
enzyme expression and activity is regulated by substrate and product level via transcription repressor HdnoR
-
-
-
additional information
?
-
Q59129
enzyme expression and activity is regulated by substrate and product level via transcription repressor HdnoR
-
-
-
additional information
?
-
Q59127
organism can grow on L-nicotine since it is converted to D-nicotine by a racemase
-
-
-
additional information
?
-
Q59128
organism can grow on L-nicotine since it is converted to D-nicotine by a racemase
-
-
-
additional information
?
-
Q59129
organism can grow on L-nicotine since it is converted to D-nicotine by a racemase
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMN
-
metalloflavoprotein, protects enzyme against inhibition by acriflavine
iron-sulfur centre
subunit B carries an iron-sulfur cluster
cytochrome P450
-
small content to nicotine oxidation, cytochrome P-450-linked monooxygenase
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Molybdenum
Tungsten
-
enzyme synthesis responds to the presence of this metal ion
Molybdenum
-
enzyme synthesis responds to the presence of this metal ion
Molybdenum
subunit C contains a molybdopterin-binding domain
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Tungsten
inhibitory to enzyme activity, does not inhibit enzyme synthesis
additional information
gene repressor HdnoR binds to the 6hdno gene operator, Kd is 21 nM, and represses enzyme expression, repressor in induced by 6-hydroxy-D-nicotine and 6-hydroxy-L-nicotine in vitro and in vivo
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additional information
gene repressor HdnoR binds to the 6hdno gene operator, Kd is 21 nM, and represses enzyme expression, repressor in induced by 6-hydroxy-D-nicotine and 6-hydroxy-L-nicotine in vitro and in vivo
-
additional information
gene repressor HdnoR binds to the 6hdno gene operator, Kd is 21 nM, and represses enzyme expression, repressor in induced by 6-hydroxy-D-nicotine and 6-hydroxy-L-nicotine in vitro and in vivo
-
additional information
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riboflavin 5'-phosphate protects enzyme against acriflavine inhibition, FMN protects enzyme against acriflavine inhibition, FAD only partially effective, glutathione protects against p-chloromercuriphenylsulfonic inhibition
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Km of (S)-nicotine uptake is 0.0056 mM
-
additional information
additional information
Km of (S)-nicotine uptake is 0.0056 mM
-
additional information
additional information
Km of (S)-nicotine uptake is 0.0056 mM
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000514 - 0.000888
-
variation caused by pre-treatment with 3-methylcholanthrene, beta-naphthoflavone or phenobarbital
additional information
-
0.119 units per mg protein, unit is defined as the amount causing a decrease in absorbancy at 578 nm of 0.001 per min
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
present both as soluble and membrane-associated form
present both as soluble and membrane-associated form
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14924
x * 30011, subunit A, x * 14924, subunit B, x * 87677, subunit C, calculated
30011
x * 30011, subunit A, x * 14924, subunit B, x * 87677, subunit C, calculated
87677
x * 30011, subunit A, x * 14924, subunit B, x * 87677, subunit C, calculated
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 30011, subunit A, x * 14924, subunit B, x * 87677, subunit C, calculated
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-19°C, 1 month, without thawing and refreezing, without loss of activity
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, heat denaturation, TEAE-cellulose chromatography
-
ammonium sulfate precipitation, ion-exchange, gel filtration; hydroxylapatite column
-
protamine sulfate and ammonium sulfate precipitation, gel filtration, ion-exchange
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene 6hdno of pAO1, DNA and amino acid sequence determination and analysis, sequence comparisons, genetic organization
gene 6hdno of pAO1, DNA sequence analysis, genetic organization, primer extension analysis, transcriptional analysis, binding and regulatory role of repressor HdnoR, effector protein IR1 is involved, overview
gene nox, DNA and amino acid sequence deteremination and analysis, recombinant expression from a broad-host-range cloning vector in Escherichia coli strain DH5alpha and Pseudomonas putida strain KT2440, the enzyme is exxpressed in both hosts but only active in Pseudomonas putida
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of all subunits requires the presence of nicotine and molybdenum in the culture medium
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H456R
additional information
additional information
construction of the nox deletion mutant strain, that loses the ability to degrade nicotine, but not pseudooxynicotine
additional information
-
construction of the nox deletion mutant strain, that loses the ability to degrade nicotine, but not pseudooxynicotine
-
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LINKS TO OTHER DATABASES (specific for EC-Number 1.5.99.4)
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