BRENDA - Enzyme Database
show all sequences of 1.13.12.16

The nonoxidative conversion of nitroethane to ethylnitronate in Neurospora crassa 2-nitropropane dioxygenase is catalyzed by Histidine 196

Francis, K.; Gadda, G.; Biochemistry 47, 9136-9144 (2008)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expression in Escherichia coli
Neurospora crassa
Engineering
Protein Variants
Commentary
Organism
H196N
the H196N variant form of the enzyme does to catalyze the formation of ethylnitronate from nitroethane. The H196N variant is a better catalyst than the wild-type enzyme for oxidative turnover with ethylnitronate
Neurospora crassa
H196N
site-directed mutagenesis, does to catalyze the formation of ethylnitronate from nitroethane. It is a better catalyst than the wild-type enzyme for oxidative turnover with ethylnitronate
Neurospora crassa
Inhibitors
Inhibitors
Commentary
Organism
Structure
ethylnitronate
-
Neurospora crassa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Km-value for O2 (wild-type enzyme) is below 0.005 mM
Neurospora crassa
0.005
-
O2
30C, pH 8, wild-type enzyme, ethylnitronate as a substrate
Neurospora crassa
0.034
-
O2
30C, pH 8, mutant enzyme H196N
Neurospora crassa
0.034
-
O2
30C, pH 8, mutant enzyme H196N, ethylnitronate as a substrate
Neurospora crassa
11
-
ethylnitronate
30C, pH 9.5, mutant enzyme H196N
Neurospora crassa
15.9
-
ethylnitronate
30C, pH 9.5, wild-type enzyme
Neurospora crassa
Organism
Organism
UniProt
Commentary
Textmining
Neurospora crassa
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Neurospora crassa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
ethyl nitronate + O2
-
685283
Neurospora crassa
? + nitrite
-
-
-
?
additional information
2-nitropropane dioxygenase utilizes a branched catalytic mechanism with nitroethane as substrate. The branch point occurs at the enzyme-ethylnitronate complex and involves either the release of the nitronate or an oxidative denitrification reaction. The partitioning of the enzyme-nitronate complex results in the formation of multiple products from independent catalytic pathways with nitroethane as substrate for the enzyme. In the nonoxidative pathway, nitroethane is deprotonated by histidine 196 to generate ethylnitronate which is subsequently released from the enzyme as a reaction product
685283
Neurospora crassa
?
-
-
-
?
nitroethane + O2
2-nitropropane dioxygenase utilizes a branched catalytic mechanism with nitroethane as substrate. The branch point occurs at the enzyme-ethylnitronate complex and involves either the release of the nitronate or an oxidative denitrification reaction. The partitioning of the enzyme-nitronate complex results in the formation of multiple products from independent catalytic pathways with nitroethane as substrate for the enzyme. In the nonoxidative pathway, nitroethane is deprotonated by histidine 196 to generate ethylnitronate which is subsequently released from the enzyme as a reaction product. The oxidative denitrification pathway was established in previous studies of the enzyme and involves the oxidation of ethylnitronate by the enzyme bound flavin to generate acetaldehyde and nitrite as product
685283
Neurospora crassa
acetaldehyde + nitrite
-
-
-
?
nitroethane + O2
2-nitropropane dioxygenase utilizes a branched catalytic mechanism with nitroethane as substrate. The branch point occurs at the enzyme-ethylnitronate complex and involves either the release of the nitronate or an oxidative denitrification reaction. The partitioning of the enzyme-nitronate complex results in the formation of multiple products from independent catalytic pathways with nitroethane as substrate for the enzyme. In the nonoxidative pathway, nitroethane is deprotonated by histidine 196 to generate ethylnitronate which is subsequently released from the enzyme as a reaction product. The oxidative denitrification pathway was established in previous studies of the enzyme and involves the oxidation of ethylnitronate by the enzyme bound flavin to generate acetaldehyde and nitrite as product
685283
Neurospora crassa
ethylnitronate
-
-
-
r
nitroethane + O2
-
685283
Neurospora crassa
? + nitrite
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
2-nitropropane dioxygenase
-
Neurospora crassa
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Neurospora crassa
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
16.2
-
ethylnitronate
30C, pH 9.5, wild-type enzyme
Neurospora crassa
185
-
ethylnitronate
30C, pH 9.5, mutant enzyme H196N
Neurospora crassa
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9.5
-
assay at
Neurospora crassa
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6
10
assays are carried out at pH 6, 8, 9.5, and 10
Neurospora crassa
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
1.2
-
ethylnitronate
30C, pH 9.5, mutant enzyme H196N
Neurospora crassa
100
-
ethylnitronate
30C, pH 9.5, wild-type enzyme
Neurospora crassa
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Neurospora crassa
Engineering (protein specific)
Protein Variants
Commentary
Organism
H196N
the H196N variant form of the enzyme does to catalyze the formation of ethylnitronate from nitroethane. The H196N variant is a better catalyst than the wild-type enzyme for oxidative turnover with ethylnitronate
Neurospora crassa
H196N
site-directed mutagenesis, does to catalyze the formation of ethylnitronate from nitroethane. It is a better catalyst than the wild-type enzyme for oxidative turnover with ethylnitronate
Neurospora crassa
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
ethylnitronate
-
Neurospora crassa
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
1.2
-
ethylnitronate
30C, pH 9.5, mutant enzyme H196N
Neurospora crassa
100
-
ethylnitronate
30C, pH 9.5, wild-type enzyme
Neurospora crassa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Km-value for O2 (wild-type enzyme) is below 0.005 mM
Neurospora crassa
0.005
-
O2
30C, pH 8, wild-type enzyme, ethylnitronate as a substrate
Neurospora crassa
0.034
-
O2
30C, pH 8, mutant enzyme H196N
Neurospora crassa
0.034
-
O2
30C, pH 8, mutant enzyme H196N, ethylnitronate as a substrate
Neurospora crassa
11
-
ethylnitronate
30C, pH 9.5, mutant enzyme H196N
Neurospora crassa
15.9
-
ethylnitronate
30C, pH 9.5, wild-type enzyme
Neurospora crassa
Purification (Commentary) (protein specific)
Commentary
Organism
-
Neurospora crassa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
ethyl nitronate + O2
-
685283
Neurospora crassa
? + nitrite
-
-
-
?
additional information
2-nitropropane dioxygenase utilizes a branched catalytic mechanism with nitroethane as substrate. The branch point occurs at the enzyme-ethylnitronate complex and involves either the release of the nitronate or an oxidative denitrification reaction. The partitioning of the enzyme-nitronate complex results in the formation of multiple products from independent catalytic pathways with nitroethane as substrate for the enzyme. In the nonoxidative pathway, nitroethane is deprotonated by histidine 196 to generate ethylnitronate which is subsequently released from the enzyme as a reaction product
685283
Neurospora crassa
?
-
-
-
?
nitroethane + O2
2-nitropropane dioxygenase utilizes a branched catalytic mechanism with nitroethane as substrate. The branch point occurs at the enzyme-ethylnitronate complex and involves either the release of the nitronate or an oxidative denitrification reaction. The partitioning of the enzyme-nitronate complex results in the formation of multiple products from independent catalytic pathways with nitroethane as substrate for the enzyme. In the nonoxidative pathway, nitroethane is deprotonated by histidine 196 to generate ethylnitronate which is subsequently released from the enzyme as a reaction product. The oxidative denitrification pathway was established in previous studies of the enzyme and involves the oxidation of ethylnitronate by the enzyme bound flavin to generate acetaldehyde and nitrite as product
685283
Neurospora crassa
acetaldehyde + nitrite
-
-
-
?
nitroethane + O2
2-nitropropane dioxygenase utilizes a branched catalytic mechanism with nitroethane as substrate. The branch point occurs at the enzyme-ethylnitronate complex and involves either the release of the nitronate or an oxidative denitrification reaction. The partitioning of the enzyme-nitronate complex results in the formation of multiple products from independent catalytic pathways with nitroethane as substrate for the enzyme. In the nonoxidative pathway, nitroethane is deprotonated by histidine 196 to generate ethylnitronate which is subsequently released from the enzyme as a reaction product. The oxidative denitrification pathway was established in previous studies of the enzyme and involves the oxidation of ethylnitronate by the enzyme bound flavin to generate acetaldehyde and nitrite as product
685283
Neurospora crassa
ethylnitronate
-
-
-
r
nitroethane + O2
-
685283
Neurospora crassa
? + nitrite
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Neurospora crassa
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
16.2
-
ethylnitronate
30C, pH 9.5, wild-type enzyme
Neurospora crassa
185
-
ethylnitronate
30C, pH 9.5, mutant enzyme H196N
Neurospora crassa
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9.5
-
assay at
Neurospora crassa
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6
10
assays are carried out at pH 6, 8, 9.5, and 10
Neurospora crassa
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.001
-
O2
30C, pH 8, wild-type enzyme
Neurospora crassa
0.0055
-
O2
30C, pH 8, mutant enzyme H196N
Neurospora crassa
1.02
-
ethylnitronate
30C, pH 8, wild-type enzyme
Neurospora crassa
16.8
-
ethylnitronate
30C, pH 8, mutant enzyme H196N
Neurospora crassa
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.001
-
O2
30C, pH 8, wild-type enzyme
Neurospora crassa
0.0055
-
O2
30C, pH 8, mutant enzyme H196N
Neurospora crassa
1.02
-
ethylnitronate
30C, pH 8, wild-type enzyme
Neurospora crassa
16.8
-
ethylnitronate
30C, pH 8, mutant enzyme H196N
Neurospora crassa
Other publictions for EC 1.13.12.16
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
745219
Vercammen
Pseudomonas aeruginosa LysR P ...
Pseudomonas aeruginosa
J. Bacteriol.
197
1026-1039
2015
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1
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1
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2
2
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-
745306
Salvi
The combined structural and k ...
Pseudomonas aeruginosa
J. Biol. Chem.
289
23764-23775
2014
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1
1
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4
-
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1
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10
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1
1
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8
1
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8
1
1
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3
1
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-
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3
3
-
6
6
727018
Smitherman
Evidence for a transient perox ...
Cyberlindnera saturnus
Biochemistry
52
2694-2704
2013
-
-
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-
-
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-
6
-
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3
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1
2
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1
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6
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2
-
2
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5
1
-
-
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-
-
-
-
6
6
728077
Klinkenberg
Rv1894c is a novel hypoxia-ind ...
Mycobacterium tuberculosis
J. Infect. Dis.
207
1525-1534
2013
-
-
1
-
1
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1
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10
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1
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1
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1
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1
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1
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1
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-
726808
Francis
A novel activity for fungal ni ...
Cyberlindnera saturnus, Neurospora crassa
Arch. Biochem. Biophys.
521
84-89
2012
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3
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10
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3
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2
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2
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3
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-
3
-
2
-
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3
2
-
-
-
-
3
3
-
3
3
724175
Li
Crystal structure and site-dir ...
Streptomyces ansochromogenes
Biochem. Biophys. Res. Commun.
405
344-348
2011
-
-
1
1
3
-
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-
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2
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3
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3
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3
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-
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1
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-
-
-
-
-
695891
Gadda
Nitronate monooxygenase, a mod ...
Cyberlindnera saturnus, Neurospora crassa, Pseudomonas aeruginosa, Cyberlindnera saturnus mrakii
Arch. Biochem. Biophys.
493
53-61
2009
-
-
-
-
-
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-
1
-
3
-
13
-
6
-
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3
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16
1
3
3
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3
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3
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3
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1
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3
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13
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16
1
3
-
-
-
3
-
-
-
-
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-
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-
696315
Francis
Inflated kinetic isotope effec ...
Neurospora crassa
Biochemistry
48
2403-2410
2009
-
-
-
-
-
-
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6
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1
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684712
Mijatovic
Oxidation of alkyl nitronates ...
Cyberlindnera mrakii
Arch. Biochem. Biophys.
473
61-68
2008
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1
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1
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1
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6
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8
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1
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8
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1
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2
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6
6
685283
Francis
The nonoxidative conversion of ...
Neurospora crassa
Biochemistry
47
9136-9144
2008
-
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1
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2
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1
6
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4
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6
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1
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2
1
1
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4
4
672094
Francis
Probing the chemical steps of ...
Neurospora crassa
Biochemistry
45
13889-13898
2006
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1
11
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1
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1
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1
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1
1
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1
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1
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1
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11
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1
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4
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1
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5
1
1
-
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-
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7
7
674590
Ha
Crystal structure of 2-nitropr ...
Pseudomonas aeruginosa
J. Biol. Chem.
281
18660-18667
2006
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1
1
4
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1
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1
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1
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2
2
1
1
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1
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1
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1
1
1
4
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1
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1
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2
2
1
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1
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656289
Francis
Involvement of a flavosemiquin ...
Neurospora crassa
J. Biol. Chem.
280
5195-5204
2005
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3
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11
-
2
4
1
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7
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3
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5
1
33
2
1
2
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28
2
1
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3
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3
3
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11
-
2
4
1
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3
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5
1
33
2
2
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28
2
1
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10
10
639233
Gadda
Substrate specificity of a nit ...
Fusarium oxysporum
Arch. Biochem. Biophys.
363
309-313
1999
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1
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1
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3
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14
-
1
1
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2
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1
2
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1
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2
2
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1
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14
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1
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2
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2
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1
1
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20
1
1
1
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9
1
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2
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2
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15
-
10
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2
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2
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1
1
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20
1
1
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9
1
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1
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1
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1
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1
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697294
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8
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8
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639222
Kido
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2-Nitropropane dioxygenase fro ...
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2
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23
2
1
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4
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2
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2
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21
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2
2
1
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2
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2
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23
2
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4
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639226
Kido
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Characterization of primary ni ...
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1
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4
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1
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1
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1
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1
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1
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4
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639227
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1984
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2
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1
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9
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1
1
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8
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1
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1
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1
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1
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14
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2
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1
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1
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8
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1
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639224
Kido
Properties of 2-nitropropane d ...
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1978
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19
2
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11
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1
2
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2
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1
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1
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1
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20
-
2
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1
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2
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639225
Kido
Purification and properties of ...
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53-58
1978
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6
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2
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4
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-
2
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-
1
1
1
14
1
1
2
2
6
-
1
-
1
3
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-
-
-
-
-
3
-
-
-
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11
-
6
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2
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2
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1
1
1
14
1
2
2
6
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1
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1
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639223
Kido
A new oxygenase, 2-nitropropan ...
Cyberlindnera mrakii, Cyberlindnera mrakii IF0 0895
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3
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13
7
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1
4
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8
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1
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17
1
1
1
1
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2
2
-
2
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3
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2
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3
-
18
-
7
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1
4
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1
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17
1
1
1
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2
2
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639235
Kido
Purification and properties of ...
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1976
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5
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1
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1
1
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5
1
1
1
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2
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1
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1
1
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5
1
1
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2
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