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Information on EC 1.5.3.5 - (S)-6-hydroxynicotine oxidase and Organism(s) Paenarthrobacter nicotinovorans and UniProt Accession Q93NH4
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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
-
monoamine
- flavoproteins
-
hydride
- 6-hydroxypseudooxynicotine
-
dehydrogenation
- pseudooxynicotine
-
d-specific
- pyrrolidine
-
dithionite-reduced
-
carbon-carbon
-
self-formed
-
fad-binding
-
s-nicotine
-
l-enantiomer
-
fitzpatrick
-
carbon-nitrogen
- isoalloxazine
- 6-hdno
-
substrate-reduced
The taxonomic range for the selected organisms is: Paenarthrobacter nicotinovorans
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
nica2, 6-hydroxy-l-nicotine oxidase, 6-hlno, 6hlno, l-6-hydroxynicotine oxidase, (s)-6-hydroxynicotine oxidase, flavoprotein nicotine oxidoreductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6-hydroxy-L-nicotine oxidase
6-hydroxy-L-nicotine:oxygen oxidoreductase
-
-
-
-
L-6-hydroxynicotine oxidase
6-hydroxy-L-nicotine oxidase
-
-
-
-
L-6-hydroxynicotine oxidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
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).
CAS REGISTRY NUMBER
COMMENTARY
37256-29-4
-
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
absolute stereospecificity on the L-form
intermediate product 6-hydroxy-N-methylmyosmine, which hydrolyzes to 6-hydroxy-pseudooxynicotine
-
?
(S)-nicotine + H2O + O2
N-methylmyosmine + H2O2
-
-
-
?
(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
-
-
-
-
?
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
-
the enzyme catalyzes the oxidation of (S)-6-hydroxynicotine to 6-hydroxypseudooxynicotine during microbial catabolism of nicotine
-
-
?
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
-
-
?
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-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
absolute stereospecificity on the L-form
-
-
?
(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
-
the enzyme catalyzes the oxidation of (S)-6-hydroxynicotine to 6-hydroxypseudooxynicotine during microbial catabolism of nicotine
-
-
?
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
?
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
the FAD content of freshly prepared wild type enzyme averages 0.17 mol FAD per mol enzyme. The FAD content of MBP-tagged enzyme averages 0.8 mol FAD per mol of enzyme
FAD
-
1 FAD per subunit, non-covalently bound
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-chloromercuriphenylsulfonate
-
60% inhibition at 0.025 mM, inhibition can be reversed by an excess of thiol compounds
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
(S)-6-hydroxynicotine
pH and temperature not specified in the publication
2.7
(S)-6-hydroxynicotine
mutant R274A/Y311W/C417W, pH 7.4, 22°C
13
(S)-nicotine
mutant R274A/Y311W/C417W, pH 7.4, 37°C
16
(S)-nicotine
mutant R274A/Y311W/C417W, pH 7.4, 22°C
0.011
(S)-6-hydroxynicotine
-
pH 7.0, 25°C, mutant enzyme K287M
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.5
(S)-6-hydroxynicotine
mutant R274A/Y311W/C417W, pH 7.4, 22°C
1.14
(S)-nicotine
mutant R274A/Y311W/C417W, pH 7.4, 37°C
2.65
(S)-nicotine
mutant R274A/Y311W/C417W, pH 7.4, 22°C
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.26
(S)-6-hydroxynicotine
mutant R274A/Y311W/C417W, pH 7.4, 22°C
0.0204
(S)-nicotine
mutant R274A/Y311W/C417W, pH 7.4, 22°C
0.0877
(S)-nicotine
mutant R274A/Y311W/C417W, pH 7.4, 37°C
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
(R)-6-hydroxynicotine
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
resiudes Asn166, Tyr311, and Lys287 as well as an active site water molecule have roles in the catalysis of the enzyme. A hydride transfer mechanism is the only viable mechanism for catalysis. During the hydride transfer process an active site water molecule bridges FAD and Lys287 through H-bonding interaction. A series of H-bonding interactions coupled with van der Waals interactions keep FAD and substrate S-6-hydroxynicotine closer. FAD achieves a bent conformation
metabolism
physiological function
-
expression of the 6-hydroxy-L-nicotine oxidase gene allows the bacterium to take up L-nicotine
additional information
metabolism
-
the enzyme catalyzes the oxidation of (S)-6-hydroxynicotine to 6-hydroxypseudooxynicotine during microbial catabolism of 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
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). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
the active enzyme exists as a stable dimer in solution
homodimer
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
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D166Q
mutation slightly reduces the KM for nicotine, it also reduced enzyme turnover by 5fold with nicotine
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
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
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
additional information
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
-
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, saturated ammonium sulfate solution, 2 weeks, little inactivation
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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
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
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
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
Decker, K.; Dai, V.D.; Mhler, H.; Bruhmuller, M.
D- and L-6-hydroxynicotine oxidase, enantioenzymes of Arthrobacter oxidans
Z. Naturforsch. B
27
1072-1073
1972
Paenarthrobacter nicotinovorans
Palmer, G.; Massey, V.
Mechanisms of flavoprotein catalysis
Biol. Oxidations (Singer, T. P. , ed. )
263-300
1968
Paenarthrobacter nicotinovorans
-
Dai, V.D.; Decker, K.; Sund, H.
Purification and properties of L-6-hydroxynicotine oxidase
Eur. J. Biochem.
4
95-102
1968
Paenarthrobacter nicotinovorans
Decker, K.; Dai, V.D.
Mechanism and specifcity of L- and D-6-hydroxynicotine oxidase
Eur. J. Biochem.
3
132-138
1967
Paenarthrobacter nicotinovorans
Decker, K.; Bleeg, H.
Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxidans
Biochim. Biophys. Acta
105
313-324
1965
Paenarthrobacter nicotinovorans
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
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
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
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
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
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
Deay, D.I.; Colvert, K.; Gao, F.; Seibold, S.; Goyal, P.; Aillon, D.; Petillo, P.; Richter, M.
An active site mutation in 6-hydroxy-L-nicotine oxidase from Arthrobacter nicotinovorans changes the substrate specificity in favor of (S)-nicotine
Arch. Biochem. Biophys.
692
108520
2020
Paenarthrobacter nicotinovorans (Q93NH4), Paenarthrobacter nicotinovorans
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