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EC Tree
Synonyms
nitronate monooxygenase, NMO,
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nitronate monooxygenase
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nitronate monooxygenase
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nitronate monooxygenase
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nitronate monooxygenase
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nitronate monooxygenase
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NMO
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2 butyl-1-nitronate + O2
2 butanal + 2 nitrite
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2 ethylnitronate + O2
2 ethanal + 2 nitrite
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2 propyl-1-nitronate + O2
2 propanal + 2 nitrite
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ethyl nitronate + O2
ethanal + nitrite
nitroethane + O2
ethanal + nitrite
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additional information
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ethyl nitronate + O2
ethanal + nitrite
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ethyl nitronate + O2
ethanal + nitrite
in the oxidative pathway, the transfer of a single electron oxidizes the organic substrate and reduces the enzyme-bound flavin to an anionic semiquinone species
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additional information
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kinetic evidence for an anion binding pocket in the active site of nitronate monooxygenase
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additional information
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only alkyl nitronates are used as substrates in the oxidative denitrification reaction. Nitroalkanes are not substrates. The enzyme is a monooxygenase
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additional information
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both the neutral and anionic forms of nitroalkanes act as substrates for the oxidative denitrification reaction. The enzyme is a monooxygenase
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additional information
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kinetic evidence for an anion binding pocket in the active site of nitronate monooxygenase
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FMN
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binding of sodium nitrite to the enzyme enzymes induces spectral changes in the FMN cofactor bound at the active site of the enzyme
FMN
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binding of sodium nitrite to the enzyme enzymes induces spectral changes in the FMN cofactor bound at the active site of the enzyme
FMN
non-covalently bound flavin cofactor, the enzyme contains one mol of FMN per mol of subunit, the enzyme utilizes a histidine in the active site to abstract the alpha-proton of neutral substrates and to stabilize the transient anionic flavosemiquinone that forms during turnover
FMN
non-covalently bound flavin cofactor, the enzyme contains one mole of FMN per mole of subunit
FMN
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the enzyme contains one mol of FMN per mol of subunit
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Butanal
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competitive inhibitor with respect to ethylnitronate as substrate
hexanal
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competitive inhibitor with respect to ethylnitronate as substrate
pentanal
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competitive inhibitor with respect to ethylnitronate as substrate
propanal
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competitive inhibitor with respect to ethylnitronate as substrate
KBr
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competitive inhibitor with respect to ethylnitronate as substrate
KCl
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competitive inhibitor with respect to ethylnitronate as substrate
KF
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competitive inhibitor with respect to ethylnitronate as substrate
KI
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competitive inhibitor with respect to ethylnitronate as substrate
NaNO2
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competitive inhibitor with respect to ethylnitronate as substrate
NaNO2
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competitive inhibitor with respect to ethylnitronate as substrate
NaNO3
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competitive inhibitor with respect to ethylnitronate as substrate
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additional information
additional information
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kinetic parameters of reductive half reaction
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additional information
additional information
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kinetic parameters of reductive half reaction
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60
Butanal
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pH 7.4, 30°C
60
hexanal
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pH 7.4, 30°C
58
pentanal
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pH 7.4, 30°C
58
propanal
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pH 7.4, 30°C
4
KBr
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pH 7.4, 30°C
11.3
KCl
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pH 7.4, 30°C
77
KF
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pH 7.4, 30°C
0.95
KI
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pH 7.4, 30°C
1.7
NaNO3
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pH 7.4, 30°C
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brenda
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UniProt
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brenda
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SwissProt
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expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
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Gadda, G.; Francis, K.
Nitronate monooxygenase, a model for anionic flavin semiquinone intermediates in oxidative catalysis
Arch. Biochem. Biophys.
493
53-61
2009
Pseudomonas aeruginosa, Neurospora crassa (Q01284), Cyberlindnera mrakii (Q12723)
brenda
Francis, K.; Gadda, G.
Kinetic evidence for an anion binding pocket in the active site of nitronate monooxygenase
Bioorg. Chem.
37
167-172
2009
Cyberlindnera mrakii, Neurospora crassa
brenda
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