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Information on EC 1.13.11.32 - 2-nitropropane dioxygenase
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.13.11.32
transferred to EC 1.13.12.16
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RECOMMENDED NAME
GeneOntology No.
2-nitropropane dioxygenase
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
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
?
-
-
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
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-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMN
non-covalently bound flavin cofactor, the enzyme contains one mole of FMN per mole of subunit
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
-
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
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
NaNO2
-
competitive inhibitor with respect to ethylnitronate as substrate
NaNO3
-
competitive inhibitor with respect to ethylnitronate as substrate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic parameters of reductive half reaction
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic parameters of reductive half reaction
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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LINKS TO OTHER DATABASES (specific for EC-Number 1.13.11.32)
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