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Information on EC 1.7.3.1 - nitroalkane oxidase and Organism(s) Fusarium oxysporum and UniProt Accession Q8X1D8
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1.7.3.1 nitroalkane oxidaseIUBMB Comments
Has an absolute requirement for FAD . While nitroethane may be the physiological substrate , the enzyme also acts on several other nitroalkanes, including 1-nitropropane, 2-nitropropane, 1-nitrobutane, 1-nitropentane, 1-nitrohexane, nitrocyclohexane and some nitroalkanols . Differs from EC 1.13.11.16, nitronate monooxygenase, in that the preferred substrates are neutral nitroalkanes rather than anionic nitronates .
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The taxonomic range for the selected organisms is: Fusarium oxysporum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
nao, nitroalkane oxidase, pa4202, nitroalkane-oxidizing enzyme, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
nitroethane oxidase
nitroethane:oxygen oxidoreductase
-
-
-
-
oxidase, nitroethane
-
-
-
-
additional information
nitroethane oxidase
-
-
-
-
additional information
-
enzyme belongs to the acyl-CoA dehydrogenase family of enzymes
additional information
-
enzyme belongs to the acyl-CoA dehydrogenase family of enzymes
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a nitroalkane + H2O + O2 = an aldehyde or ketone + nitrite + H2O2
mechanism
-
a nitroalkane + H2O + O2 = an aldehyde or ketone + nitrite + H2O2
ping pong kinetic mechanism
-
a nitroalkane + H2O + O2 = an aldehyde or ketone + nitrite + H2O2
Asp402 acts as the active site base of the enzyme, mechanism, substrate CH-bond cleavage is rate limiting for the reduction of the enzyme by nitroethane
-
a nitroalkane + H2O + O2 = an aldehyde or ketone + nitrite + H2O2
Asp402 acts as the active site base of the enzyme, mechanism: catalysis is initiated by the active site base Asp402 that deprotonates the neutral substrate to yield a carbanion that can attack the N-5 position of the oxidized flavin, CH-bond cleavage is rate limiting for the reduction of the enzyme by nitroethane
-
a nitroalkane + H2O + O2 = an aldehyde or ketone + nitrite + H2O2
detailed mechanism, with carbanion reaction intermediate formation, an aspartate residue is the active site base, substrate CH-bond cleavage is rate limiting for the reduction of the enzyme by nitroethane, the active site of the enzyme is a hydrophobic channel, tunneling, overview
-
a nitroalkane + H2O + O2 = an aldehyde or ketone + nitrite + H2O2
mechanism, involves removal of a proton from the nitroalkane, forming a carbanion which adds to the N5 of the flavin, elimination of nitrite from the resulting adduct forms an electrophilic imine intermediate which can be attacked by hydroxide
-
a nitroalkane + H2O + O2 = an aldehyde or ketone + nitrite + H2O2
mechanism, transition-state stabilization is essential, protein-substrate interactions in the transition state, reaction involves quantum mechaniscal tunneling, Asp402 is involved in initial abstraction of a proton from the neutral substrate, overview
-
a nitroalkane + H2O + O2 = an aldehyde or ketone + nitrite + H2O2
critical importance of the interaction between Asp402 and Arg409 for proton abstraction by nitroalkane oxidase
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
nitroalkane:oxygen oxidoreductase
Has an absolute requirement for FAD [4]. While nitroethane may be the physiological substrate [2], the enzyme also acts on several other nitroalkanes, including 1-nitropropane, 2-nitropropane, 1-nitrobutane, 1-nitropentane, 1-nitrohexane, nitrocyclohexane and some nitroalkanols [4]. Differs from EC 1.13.11.16, nitronate monooxygenase, in that the preferred substrates are neutral nitroalkanes rather than anionic nitronates [4].
CAS REGISTRY NUMBER
COMMENTARY
9029-36-1
-
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
nitroethane + H2O
ethanal + nitrite + H2O2
solvent isotope and viscositiy effects: the kcat proton inventory is consistent with a single exchangeable proton in flight, while the kcat/KM is consistent with either a single proton in flight in the transition state or a medium effect. Increasing the solvent viscosity does not affect the kcat or kcat/KM value significantly, establishing that nitroethane binding is at equilibrium and that product release does not limit kcat
-
-
?
nitroalkane + O2 + H2O
aldehyde or ketone + nitrite + H2O2
-
neutral nitroalkanes
-
-
?
nitroethane + H2O + O2
acetaldehyde + nitrite + H2O2
-
-
-
-
?
1-nitrobutane + O2 + H2O
butyraldehyde + nitrite + H2O2
-
-
-
-
?
1-nitrobutane + O2 + H2O
butyraldehyde + nitrite + H2O2
-
400fold more effective than nitroethane
-
-
?
nitroethane + O2
acetaldehyde + HNO2
-
at pH 7, bi-ter ping-pong mechanism with oxygen reacting with the free reduced enzyme after release of the aldehyde product
-
-
?
nitroethane + O2 + H2O
ethanal + nitrite + H2O2
-
nitroethane is the only substrate, of diverse primary and secondary alkanes, for which deprotonation is fully rate limiting for the reductive half reaction
-
-
?
nitroethane + O2 + H2O
ethanal + nitrite + H2O2
-
O2 is delivered from air-saturated buffer in the assay reaction
-
-
?
nitroethane + O2 + H2O
ethanal + nitrite + H2O2
-
substrate CH-bond cleavage is rate limiting for the reduction of the enzyme by nitroethane
-
-
?
nitroethane + O2 + H2O
ethanal + nitrite + H2O2
-
the neutral substrate form is preferred, 5fold lower activity with the substrate anion, the D402 mutant enzymes in contrast prefer the anionic substrate form
-
-
?
additional information
?
-
-
the physiological role of the enzyme is the oxidation of nitroaliphatic species
-
-
?
additional information
?
-
-
analysis of reaction intermediates formed by mass spectrometry and gel filtration
-
-
?
additional information
?
-
-
enzyme catalyzes the oxidation of nitroalkanes to the respective aldehydes or ketones with consumption of molecular oxygen and releasing nitrite and hydrogen peroxide
-
-
?
additional information
?
-
-
enzyme catalyzes the oxidation of primary and secondary nitroalkanes to the respective aldehydes or ketones, releasing nitrite
-
-
?
additional information
?
-
-
enzyme does not require anionic nitroalkanes for activity, enzyme catalyzes the oxidation of a number of primary and secondary nitroalkanes to the respective aldehydes or ketones with preference for primary nitroalkanes, monotonic increase with each additional methylene group from nitroethane to 1-nitrobutane increasing kcat/Km value by 20fold, no further increase with 1-nitropentane and 1-nitrohexane
-
-
?
additional information
?
-
-
enzyme shows high substrate specificity
-
-
?
additional information
?
-
-
the enzyme does not oxidize acyl-CoA substrates and prefers primary nitroalkanes containing four or more carbon atoms
-
-
-
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
additional information
?
-
-
the physiological role of the enzyme is the oxidation of nitroaliphatic species
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
FAD in the recombinant enzyme is in the oxidized state, with a spectrum indistinguishable from that of the activated form of the nonrecombinant enzyme
FAD
-
1 mol of FAD per mol of subunit is required for catalysis, reversible removal of FAD yields inactive enzyme
FAD
-
absolutely required, binding structure, involving Ser171, and reactive structure analysis, the apoenzyme is inactive, removal of cofactor in its active form is reversible
FAD
-
formation of 5-nitroalkyl-FAD intermediates, structure in cyanide inactivated enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetaldehyde
-
noncompetitive inhibitor versus nitroethane due to formation of a dead-end complex between the oxidized enzyme and the product, competitive inhibitor versus oxygen
Butyraldehyde
-
noncompetitive inhibitor versus nitroethane due to formation of a dead-end complex between the oxidized enzyme and the product
cyanide
-
inactivation of the enzyme by trapping of the electrophilic imine reaction intermediate, formation of a cyanoalkyl intermediate, reaction with the substrate after proton abstraction but before flavin oxidation
nitroethane
-
substrate inhibition detected in mutant enzyme R409K, no substrate inhibition is detected in mutant enzyme D402E
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
imidazole
-
unprotonated imidazole causes a 5fold increase in maximal velocity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.9
nitroethane
-
mutant enzyme S171V, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
2
nitroethane
-
mutant enzyme C397S, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
2
nitroethane
-
mutant enzyme S171T, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
2.1
nitroethane
-
mutant enzyme S171A, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
2.3
nitroethane
-
wild type enzyme, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
4.8
nitroethane
-
mutant enzyme Y398F, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
0.011
O2
-
mutant enzyme S171T, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
0.028
O2
-
mutant enzyme Y398F, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
0.029
O2
-
mutant enzyme S171A, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
0.044
O2
-
mutant enzyme S171V, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
0.058
O2
-
mutant enzyme C397S, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
additional information
additional information
-
kinetic competency of the cationic imine enzyme intermediate
-
additional information
additional information
-
kinetics and thermodynamics of the deprotonation step with substrate nitroethane, effects of tunneling
-
additional information
additional information
-
steady-state and rapid reaction kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
thermodynamics, kinetic mechanism with nitroethane and 1-nitrobutane, isotopic effects, monotonic increase with each additional methylene group from nitroethane to 1-nitrobutane increasing kcat/Km value by 20fold, no further increase with 1-nitropentane and 1-nitrohexane
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.4
nitroethane
-
mutant enzyme S171A, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
6.2
nitroethane
-
mutant enzyme S171V, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
7.2
nitroethane
-
mutant enzyme S171T, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
7.3
nitroethane
-
mutant enzyme C397S, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
10.6
nitroethane
-
mutant enzyme Y398F, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
15
nitroethane
-
wild type enzyme, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.2
nitroethane
-
mutant enzyme Y398F, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
2.6
nitroethane
-
mutant enzyme S171A, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
3.2
nitroethane
-
mutant enzyme S171V, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
3.6
nitroethane
-
mutant enzyme S171T, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
6.3
nitroethane
-
wild type enzyme, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
152
nitroethane
-
pH 8.0, 30°C, mutant enzyme R409K, substrate inhibition constant
additional information
additional information
-
inactivation kinetics with different substrates
-
additional information
additional information
-
Ki pH profile for competitive inhibitor valerate
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the pH-dependence of the reaction with the wild-type enzyme depends on the substrate form, at pH 7.4 activity with the neutral substrate increases while is decreases with the nitroethane anion
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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). NAO_FUSOX
439
0
48162
Swiss-Prot
other Location (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
47955
48162
-
x * 48162, amino acid sequence calculation, enzyme forms homodimers and homotetramers with a preference for the latter
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
oligomer
-
enzyme forms homodimers and homotetramers with a preference for the latter
oligomer
-
x * 48162, amino acid sequence calculation, enzyme forms homodimers and homotetramers with a preference for the latter
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization data of mutant D402N in complex with 1-nitrohexane or 1-nitrooctane show the presence of substrate in the binding site. The aliphatic chain of the substrate extends into a tunnel leading to the enzyme surface. The oxygens of the substrate nitro group interact both with amino acid residues and with the 2'-hydroxyl of the FAD. The structure of wild-type enzyme trapped with cyanide during oxidation of 1-nitrohexane shows the presence of the modified flavin. A continuous hydrogen bond network connects the nitrogen of the CN-hexyl-FAD through the FAD 2'-hydroxyl to a chain of water molecules extending to the protein surface. Data for mutant S276A in complex with nitrohexane
hexagonal rod-shaped crystals of R409K and D402E NAO were obtained using hanging drop vapor-diffusion methods
-
purified recombinant wild-type enzyme, crystallization of the native enzyme in 2 different crystal forms and of the selenomethionine-labeled enzyme in a third one, hanging drop vapour diffusion method, sodium cacodylate buffer, pH 7.5, containing spermidine hydrochloride, and PEG 4000 at varying concentrations for all 3 mixtures, crystal form 2 requires addition of 1,6-hexanediol at 8% w/v, crystal form 3 requires DTT at 10 mM, 4°C, 10-14 days, X-ray diffraction structure determinations and analysis at 3.2-2.0 A resolution or below, three-wavelength MAD data
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C397S
the mutant shows reduced activity compared to the wild type enzyme
D402E
the mutant shows severely reduced activity compared to the wild type enzyme
D402N
R409K
the mutant shows severely reduced activity compared to the wild type enzyme
S171A
the mutant shows reduced activity compared to the wild type enzyme
S276A
Y398F
the mutant shows reduced activity compared to the wild type enzyme
C397S
-
the mutation results in decreases in the rate constants for removal of the substrate proton by about 5fold and decreases in the rate constant for product release of about 2fold, the mutant enzyme is less stable than the wild type enzyme
D402A
-
site-directed mutation of the active site base, 20fold reduced catalytic efficiency with neutral nitroethane as substrate compared to the wild-type enzyme, while the wild-type enzyme prefers the neutral substrate the mutant prefers the anion substrate form, altered pH-dependence with both substrate forms compared to the wild-type enzyme
D402E
D402N
-
site-directed mutation of the active site base, 140fold reduced catalytic efficiency with neutral nitroethane as substrate compared to the wild-type enzyme, while the wild-type enzyme prefers the neutral substrate the mutant prefers the anion substrate form, altered pH-dependence with both substrate forms compared to the wild-type enzyme
R409K
S171A
-
the mutation results in decreases in the rate constants for removal of the substrate proton by about 5fold and decreases in the rate constant for product release of about 2fold
S171T
-
the mutation results in decreases in the rate constants for removal of the substrate proton by about 5fold and decreases in the rate constant for product release of about 2fold, the mutation alters the rate constant for flavin oxidation
S171V
-
the mutation results in decreases in the rate constants for removal of the substrate proton by about 5fold and decreases in the rate constant for product release of about 2fold, the mutation alters the rate constant for flavin oxidation
Y398F
-
the mutation results in decreases in the rate constants for removal of the substrate proton by about 5fold and decreases in the rate constant for product release of about 2fold, the mutant enzyme is less stable than the wild type enzyme
D402N
no detectable activity with neutral substrates. Crystallization data in complex with 1-nitrohexane or 1-nitrooctane show the presence of substrate in the binding site. The aliphatic chain of the substrate extends into a tunnel leading to the enzyme surface. The oxygens of the substrate nitro group interact both with amino acid residues and with the 2'-hydroxyl of the FAD
D402N
the mutant shows reduced activity compared to the wild type enzyme
S276A
the mutant shows severely reduced activity compared to the wild type enzyme
D402E
-
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme, mutation has no effect on the rate of reaction of the reduced enzyme with oxygen, reaction mechanism analysis
D402E
-
mutation results in a decrease in the rate constant for proton abstraction of 18fold. The structure of the D402E enzyme, determined at 2.4 A resolution, shows that there is a smaller increase in the distance between Arg409 and the carboxylate at position 402. The interaction of this residue with Ser276 is perturbed
D402E
-
the mutation results in a decrease in the rate constant for proton abstraction of 18fold. The structure of the D402E enzyme shows that there is a smaller increase in the distance between Arg409 and the carboxylate at position 402 (compared to mutant enzyme R409K), and the interaction of this residue with Ser276 is perturbed
R409K
-
the mutation results in a decrease in the rate constant for proton abstraction of 100fold. Analysis of the three-dimensional structure of the R409K enzyme shows that the critical structural change is an increase in the distance between the carboxylate of Asp402 and the positively charged nitrogen in the side chain of the residue at position 409
R409K
-
the mutation results in a decrease in the rate constant for proton abstraction of 100fold. Analysis of the three-dimensional structure of the R409K enzyme, determined by X-ray crystallography to a resolution of 2.65 A, shows that the critical structural change is an increase in the distance between the carboxylate of Asp402 and the positively charged nitrogen in the side chain of the residue at position 409
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strains BL21(DE3) and methionine auxotroph B834(DE3)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Heaseley, C.J.; Fitzpatrick, P.F.
Kinetic mechanism and substrate specificity of nitroalkane oxidase
Biochem. Biophys. Res. Commun.
225
6-10
1996
Fusarium oxysporum
Gadda, G.; Fitzpatrick, P.F.
Mechanism of nitroalkane oxidase: 2. pH and kinetic isotope effects
Biochemistry
39
1406-1410
2000
Fusarium oxysporum
Gadda, G.; Fitzpatrick, P.F.
Iso-mechanism of nitroalkane oxidase: 1. Inhibition studies and activation by imidazole
Biochemistry
39
1400-1405
2000
Fusarium oxysporum
Gadda, G.; Fitzpatrick, P.F.
Biochemical and physical characterization of the active FAD-containing form of nitroalkane oxidase from Fusarium oxysporum
Biochemistry
37
6154-6164
1998
Fusarium oxysporum
Daubner, S.C.; Gadda, G.; Valley, M.P.; Fitzpatrick, P.F.
Cloning of nitroalkane oxidase from Fusarium oxysporum identifies a new member of the acyl-CoA dehydrogenase superfamily
Proc. Natl. Acad. Sci. USA
99
2702-2707
2002
Fusarium oxysporum
Nagpal, A.; Valley, M.P.; Fitzpatrick, P.F.; Orville, A.M.
Crystallization and preliminary analysis of active nitroalkane oxidase in three crystal forms
Acta Crystallogr. Sect. D
60
1456-1460
2004
Fusarium oxysporum
Fitzpatrick, P.F.; Orville, A.M.; Nagpal, A.; Valley, M.P.
Nitroalkane oxidase, a carbanion-forming flavoprotein homologous to acyl-CoA dehydrogenase
Arch. Biochem. Biophys.
433
157-165
2005
Fusarium oxysporum
Valley, M.P.; Fitzpatrick, P.F.
Reductive half-reaction of nitroalkane oxidase: effect of mutation of the active site apartate to glutamate
Biochemistry
42
5850-5856
2003
Fusarium oxysporum
Valley, M.P.; Fitzpatrick, P.F.
Inactivation of nitroalkane oxidase upon mutation of the active site base and rescue with a deprotonated substrate
J. Am. Chem. Soc.
125
8738-8739
2003
Fusarium oxysporum
Valley, M.P.; Fitzpatrick, P.F.
Comparison of enzymatic and nonenzymatic nitroethane anion formation: thermodynamics and contribution of tunneling
J. Am. Chem. Soc.
126
6244-6245
2004
Fusarium oxysporum
Valley, M.P.; Tichy, S.E.; Fitzpatrick, P.F.
Establishing the kinetic competency of the cationic imine intermediate in nitroalkane oxidase
J. Am. Chem. Soc.
127
2062-2066
2005
Fusarium oxysporum
Nagpal, A.; Valley, M.P.; Fitzpatrick, P.F.; Orville, A.M.
Crystal structures of nitroalkane oxidase: insights into the reaction mechanism from a covalent complex of the flavoenzyme trapped during turnover
Biochemistry
45
1138-1150
2006
Fusarium oxysporum
Fitzpatrick, P.F.; Bozinovski, D.M.; Heroux, A.; Shaw, P.G.; Valley, M.P.; Orville, A.M.
Mechanistic and structural analyses of the roles of Arg409 and Asp402 in the reaction of the flavoprotein nitroalkane oxidase
Biochemistry
46
13800-13808
2007
Fusarium oxysporum
Heroux, A.; Bozinovski, D.M.; Valley, M.P.; Fitzpatrick, P.F.; Orville, A.M.
Crystal structures of intermediates in the nitroalkane oxidase reaction
Biochemistry
48
3407-3416
2009
Fusarium oxysporum (Q8X1D8)
Valley, M.P.; Fenny, N.S.; Ali, S.R.; Fitzpatrick, P.F.
Characterization of active site residues of nitroalkane oxidase
Bioorg. Chem.
38
115-119
2010
Fusarium oxysporum
Gadda, G.; Fitzpatrick, P.F.
Solvent isotope and viscosity effects on the steady-state kinetics of the flavoprotein nitroalkane oxidase
FEBS Lett.
587
2785-2789
2013
Fusarium oxysporum (Q8X1D8), Fusarium oxysporum ATCC 695 (Q8X1D8)
Torres-Guzman, J.; Padilla-Guerrero, I.; Cervantes-Quintero, K.; Martinez-Vazquez, A.; Ibarra-Guzman, M.; Gonzalez-Hernandez, G.
Peculiarities of nitronate monooxygenases and perspectives for in vivo and in vitro applications
Appl. Microbiol. Biotechnol.
105
8019-8032
2021
Fusarium oxysporum
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