We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Synonyms
nitronate monooxygenase, NMO,
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
nitronate monooxygenase
-
-
nitronate monooxygenase
-
nitronate monooxygenase
-
-
nitronate monooxygenase
-
nitronate monooxygenase
-
-
NMO
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 butyl-1-nitronate + O2
2 butanal + 2 nitrite
-
-
-
?
2 ethylnitronate + O2
2 ethanal + 2 nitrite
-
-
-
?
2 propyl-1-nitronate + O2
2 propanal + 2 nitrite
-
-
-
?
ethyl nitronate + O2
ethanal + nitrite
nitroethane + O2
ethanal + nitrite
-
-
?
additional information
?
-
ethyl nitronate + O2
ethanal + nitrite
-
-
-
?
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
-
?
additional information
?
-
-
kinetic evidence for an anion binding pocket in the active site of nitronate monooxygenase
-
?
additional information
?
-
only alkyl nitronates are used as substrates in the oxidative denitrification reaction. Nitroalkanes are not substrates. The enzyme is a monooxygenase
-
?
additional information
?
-
both the neutral and anionic forms of nitroalkanes act as substrates for the oxidative denitrification reaction. The enzyme is a monooxygenase
-
?
additional information
?
-
-
kinetic evidence for an anion binding pocket in the active site of nitronate monooxygenase
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
FMN
-
binding of sodium nitrite to the enzyme enzymes induces spectral changes in the FMN cofactor bound at the active site of the enzyme
FMN
-
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
-
the enzyme contains one mol of FMN per mol of subunit
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Butanal
-
competitive inhibitor with respect to ethylnitronate as substrate
hexanal
-
competitive inhibitor with respect to ethylnitronate as substrate
pentanal
-
competitive inhibitor with respect to ethylnitronate as substrate
propanal
-
competitive inhibitor with respect to ethylnitronate as substrate
KBr
-
competitive inhibitor with respect to ethylnitronate as substrate
KCl
-
competitive inhibitor with respect to ethylnitronate as substrate
KF
-
competitive inhibitor with respect to ethylnitronate as substrate
KI
-
competitive inhibitor with respect to ethylnitronate as substrate
NaNO2
-
competitive inhibitor with respect to ethylnitronate as substrate
NaNO2
-
competitive inhibitor with respect to ethylnitronate as substrate
NaNO3
-
competitive inhibitor with respect to ethylnitronate as substrate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
additional information
-
kinetic parameters of reductive half reaction
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
additional information
-
kinetic parameters of reductive half reaction
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
60
Butanal
-
pH 7.4, 30°C
60
hexanal
-
pH 7.4, 30°C
58
pentanal
-
pH 7.4, 30°C
58
propanal
-
pH 7.4, 30°C
4
KBr
-
pH 7.4, 30°C
11.3
KCl
-
pH 7.4, 30°C
77
KF
-
pH 7.4, 30°C
0.95
KI
-
pH 7.4, 30°C
1.7
NaNO3
-
pH 7.4, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
-
SwissProt
brenda
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Select items on the left to see more content.
html completed
HOME
login
history
all enzymes
BRENDA home
History
1.13.11.32 2-nitropropane dioxygenase
more
top
Information
