BRENDA - Enzyme Database
show all sequences of 1.13.12.16

The combined structural and kinetic characterization of a bacterial nitronate monooxygenase from Pseudomonas aeruginosa PAO1 establishes NMO class I and II

Salvi, F.; Agniswamy, J.; Yuan, H.; Vercammen, K.; Pelicaen, R.; Cornelis, P.; Spain, J.C.; Weber, I.T.; Gadda, G.; J. Biol. Chem. 289, 23764-23775 (2014)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
gene pa4202, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta(DE3)pLysS
Pseudomonas aeruginosa
Crystallization (Commentary)
Crystallization (Commentary)
Organism
purified recombinant His-tagged enzyme, vapor diffusion hanging drop method at room temperature, 0.002 ml of 14 mg/ml protein in 50 mM Tris-Cl, pH 8.0, 100 mM NaCl, 20 mM 2-nitropropane, with 0.002 ml of reservoir solution containing 14% w/v PEG 5000 monomethylether and 0.1 M Na-HEPES, pH 7.0, and equilibration against 1 ml of reservoir solution, 7-10 days, X-ray diffraction structure determination and analysis at 1.44 A resolution, molecular replacement
Pseudomonas aeruginosa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
steady-state kinetic mechanism
Pseudomonas aeruginosa
0.11
-
propionate-3-nitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
5
-
ethylnitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
6
-
propyl-1-nitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
3 propionate-3-nitronate + O2
Pseudomonas aeruginosa
-
3 malonic semialdehyde + nitrite + 2 nitrate + H2O2
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Pseudomonas aeruginosa
Q9HWH9
-
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant His-tagged enzyme from Escherichia coli strain Rosetta(DE3)pLysS by affinity chromatography
Pseudomonas aeruginosa
Reaction
Reaction
Commentary
Organism
Reaction ID
ethylnitronate + O2 = acetaldehyde + nitrite + other products
catalyze the oxidation of propionate-3-nitronate or other nitronate analogues through a radical mechanism involving a catalytic flavosemiquinone without formation of a canonical C4a-(hydro)peroxyflavin
Pseudomonas aeruginosa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
3 propionate-3-nitronate + O2
-
745306
Pseudomonas aeruginosa
3 malonic semialdehyde + nitrite + 2 nitrate + H2O2
-
-
-
?
3 propionate-3-nitronate + O2
best substrate
745306
Pseudomonas aeruginosa
3 malonic semialdehyde + nitrite + 2 nitrate + H2O2
-
-
-
?
butyl-1-nitronate + O2
-
745306
Pseudomonas aeruginosa
?
-
-
-
?
ethylnitronate + O2
-
745306
Pseudomonas aeruginosa
acetaldehyde + nitrite + other products
-
-
-
?
additional information
the enzyme is active on propionate-3-nitronate and other alkyl nitronates, but cannot oxidize nitroalkanes, e.g. 3-nitropropionate, nitroethane, 1-nitropropane, 1-nitrobutane, 1-nitropentane, or 2-nitropropane. Anaerobic reduction of the enzyme with propionate-3-nitronate yields a flavosemiquinone
745306
Pseudomonas aeruginosa
?
-
-
-
?
pentyl-1-nitronate + O2
-
745306
Pseudomonas aeruginosa
?
-
-
-
?
propyl-1-nitronate + O2
-
745306
Pseudomonas aeruginosa
?
-
-
-
?
propyl-2-nitronate + O2
-
745306
Pseudomonas aeruginosa
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
the dimer interface includes eight contacts mainly in the FMN-binding domain and it does not seem to be directly relevant for catalysis as it is far from the active site pocket, structure analysis, overview
Pseudomonas aeruginosa
Synonyms
Synonyms
Commentary
Organism
NMO
-
Pseudomonas aeruginosa
Pa-NMO
-
Pseudomonas aeruginosa
PA4202
-
Pseudomonas aeruginosa
protein PA4202
-
Pseudomonas aeruginosa
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Pseudomonas aeruginosa
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
350
-
ethylnitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
1120
-
propyl-1-nitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
1300
-
propionate-3-nitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Pseudomonas aeruginosa
Cofactor
Cofactor
Commentary
Organism
Structure
FMN
dependent on, FMN-binding domain structure, overview
Pseudomonas aeruginosa
Cloned(Commentary) (protein specific)
Commentary
Organism
gene pa4202, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta(DE3)pLysS
Pseudomonas aeruginosa
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FMN
dependent on, FMN-binding domain structure, overview
Pseudomonas aeruginosa
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant His-tagged enzyme, vapor diffusion hanging drop method at room temperature, 0.002 ml of 14 mg/ml protein in 50 mM Tris-Cl, pH 8.0, 100 mM NaCl, 20 mM 2-nitropropane, with 0.002 ml of reservoir solution containing 14% w/v PEG 5000 monomethylether and 0.1 M Na-HEPES, pH 7.0, and equilibration against 1 ml of reservoir solution, 7-10 days, X-ray diffraction structure determination and analysis at 1.44 A resolution, molecular replacement
Pseudomonas aeruginosa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
steady-state kinetic mechanism
Pseudomonas aeruginosa
0.11
-
propionate-3-nitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
5
-
ethylnitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
6
-
propyl-1-nitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
3 propionate-3-nitronate + O2
Pseudomonas aeruginosa
-
3 malonic semialdehyde + nitrite + 2 nitrate + H2O2
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain Rosetta(DE3)pLysS by affinity chromatography
Pseudomonas aeruginosa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
3 propionate-3-nitronate + O2
-
745306
Pseudomonas aeruginosa
3 malonic semialdehyde + nitrite + 2 nitrate + H2O2
-
-
-
?
3 propionate-3-nitronate + O2
best substrate
745306
Pseudomonas aeruginosa
3 malonic semialdehyde + nitrite + 2 nitrate + H2O2
-
-
-
?
butyl-1-nitronate + O2
-
745306
Pseudomonas aeruginosa
?
-
-
-
?
ethylnitronate + O2
-
745306
Pseudomonas aeruginosa
acetaldehyde + nitrite + other products
-
-
-
?
additional information
the enzyme is active on propionate-3-nitronate and other alkyl nitronates, but cannot oxidize nitroalkanes, e.g. 3-nitropropionate, nitroethane, 1-nitropropane, 1-nitrobutane, 1-nitropentane, or 2-nitropropane. Anaerobic reduction of the enzyme with propionate-3-nitronate yields a flavosemiquinone
745306
Pseudomonas aeruginosa
?
-
-
-
?
pentyl-1-nitronate + O2
-
745306
Pseudomonas aeruginosa
?
-
-
-
?
propyl-1-nitronate + O2
-
745306
Pseudomonas aeruginosa
?
-
-
-
?
propyl-2-nitronate + O2
-
745306
Pseudomonas aeruginosa
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
the dimer interface includes eight contacts mainly in the FMN-binding domain and it does not seem to be directly relevant for catalysis as it is far from the active site pocket, structure analysis, overview
Pseudomonas aeruginosa
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Pseudomonas aeruginosa
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
350
-
ethylnitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
1120
-
propyl-1-nitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
1300
-
propionate-3-nitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Pseudomonas aeruginosa
General Information
General Information
Commentary
Organism
evolution
NMO is a member of the group H flavin-dependent monooxygenases
Pseudomonas aeruginosa
additional information
four conserved motifs are identified in PA4202. Oxidation of propionate-3-nitronate by NMO yields malonic semialdehyde, which is an important metabolite that can be converted to acetyl-CoA, acetate, or 3-hydroxypropionate and enter various catabolic or anabolic pathways. Active site structure analysis, overview
Pseudomonas aeruginosa
physiological function
nitronate monooxygenase oxidizes the mitochondrial toxin propionate 3-nitronate to malonate semialdehyde, and detoxifies the deadly toxin
Pseudomonas aeruginosa
General Information (protein specific)
General Information
Commentary
Organism
evolution
NMO is a member of the group H flavin-dependent monooxygenases
Pseudomonas aeruginosa
additional information
four conserved motifs are identified in PA4202. Oxidation of propionate-3-nitronate by NMO yields malonic semialdehyde, which is an important metabolite that can be converted to acetyl-CoA, acetate, or 3-hydroxypropionate and enter various catabolic or anabolic pathways. Active site structure analysis, overview
Pseudomonas aeruginosa
physiological function
nitronate monooxygenase oxidizes the mitochondrial toxin propionate 3-nitronate to malonate semialdehyde, and detoxifies the deadly toxin
Pseudomonas aeruginosa
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
29
-
propyl-2-nitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
33
-
butyl-1-nitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
70
-
ethylnitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
91
-
pentyl-1-nitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
186.71
-
propyl-1-nitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
11818.2
-
propionate-3-nitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
29
-
propyl-2-nitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
33
-
butyl-1-nitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
70
-
ethylnitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
91
-
pentyl-1-nitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
186.71
-
propyl-1-nitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
11818.2
-
propionate-3-nitronate
pH 7.5, 30°C, recombinant enzyme
Pseudomonas aeruginosa
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
-
-
1
-
1
-
-
-
-
-
-
1
-
3
-
-
-
-
-
-
-
-
1
-
5
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
745306
Salvi
The combined structural and k ...
Pseudomonas aeruginosa
J. Biol. Chem.
289
23764-23775
2014
-
-
1
1
-
-
-
4
-
-
-
1
-
10
-
-
1
1
-
-
-
-
8
1
5
1
-
-
3
1
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
4
-
-
-
1
-
-
-
1
-
-
-
-
8
1
1
-
-
3
1
-
-
-
-
3
3
-
6
6
727018
Smitherman
Evidence for a transient perox ...
Cyberlindnera saturnus
Biochemistry
52
2694-2704
2013
-
-
-
-
-
-
-
6
-
-
-
-
-
3
-
-
-
-
-
-
-
-
2
-
1
2
-
-
5
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
2
-
2
-
-
5
1
-
-
-
-
-
-
-
6
6
728077
Klinkenberg
Rv1894c is a novel hypoxia-ind ...
Mycobacterium tuberculosis
J. Infect. Dis.
207
1525-1534
2013
-
-
1
-
1
-
1
-
-
-
-
-
-
10
-
-
1
-
-
-
-
-
1
-
2
1
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
1
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
1
-
-
1
-
-
726808
Francis
A novel activity for fungal ni ...
Cyberlindnera saturnus, Neurospora crassa
Arch. Biochem. Biophys.
521
84-89
2012
-
-
-
-
-
-
-
3
-
-
-
-
-
10
-
-
-
-
-
-
-
-
3
-
4
2
-
-
3
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
3
-
2
-
-
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
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
3
-
2
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
695891
Gadda
Nitronate monooxygenase, a mod ...
Cyberlindnera saturnus, Neurospora crassa, Pseudomonas aeruginosa, Cyberlindnera saturnus mrakii
Arch. Biochem. Biophys.
493
53-61
2009
-
-
-
-
-
-
-
1
-
3
-
13
-
6
-
-
-
3
-
-
-
-
16
1
3
3
-
-
-
3
-
-
3
-
-
-
-
-
-
3
-
-
-
-
-
-
1
-
3
-
13
-
-
-
-
-
-
-
-
16
1
3
-
-
-
3
-
-
-
-
-
-
-
-
-
696315
Francis
Inflated kinetic isotope effec ...
Neurospora crassa
Biochemistry
48
2403-2410
2009
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
684712
Mijatovic
Oxidation of alkyl nitronates ...
Cyberlindnera mrakii
Arch. Biochem. Biophys.
473
61-68
2008
-
-
1
-
-
-
1
-
-
1
1
-
-
6
-
-
1
-
-
2
-
-
8
-
1
1
-
-
-
2
-
-
1
-
-
-
-
-
1
1
-
-
-
-
1
-
-
-
1
1
-
-
-
-
1
-
2
-
-
8
-
1
-
-
-
2
-
-
-
-
-
-
-
6
6
685283
Francis
The nonoxidative conversion of ...
Neurospora crassa
Biochemistry
47
9136-9144
2008
-
-
1
-
2
-
1
6
-
-
-
-
-
4
-
-
1
-
-
-
-
-
5
-
1
1
-
-
2
1
1
-
-
2
-
-
-
-
1
-
-
2
-
-
1
2
6
-
-
-
-
-
-
-
1
-
-
-
-
5
-
1
-
-
2
1
1
-
-
-
-
-
-
4
4
672094
Francis
Probing the chemical steps of ...
Neurospora crassa
Biochemistry
45
13889-13898
2006
-
-
-
-
-
-
1
11
-
-
-
-
-
1
-
-
1
-
-
-
-
-
4
-
2
1
-
-
5
1
1
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
11
-
-
-
-
-
-
-
1
-
-
-
-
4
-
1
-
-
5
1
1
-
-
-
-
-
-
7
7
674590
Ha
Crystal structure of 2-nitropr ...
Pseudomonas aeruginosa
J. Biol. Chem.
281
18660-18667
2006
-
-
1
1
4
-
1
-
-
-
1
-
-
5
-
-
1
-
-
-
-
-
2
2
1
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
1
4
-
-
1
-
-
-
-
1
-
-
-
-
1
-
-
-
-
2
2
1
-
-
-
1
-
-
-
-
-
-
-
-
-
656289
Francis
Involvement of a flavosemiquin ...
Neurospora crassa
J. Biol. Chem.
280
5195-5204
2005
-
-
3
-
-
-
-
11
-
2
4
1
-
7
-
-
3
-
-
-
5
1
33
2
1
2
-
-
28
2
1
-
3
-
-
-
-
-
3
3
-
-
-
-
-
-
11
-
2
4
1
-
-
-
3
-
-
5
1
33
2
2
-
-
28
2
1
-
-
-
-
-
-
10
10
639233
Gadda
Substrate specificity of a nit ...
Fusarium oxysporum
Arch. Biochem. Biophys.
363
309-313
1999
-
-
-
-
-
-
1
-
-
-
-
1
-
3
-
-
-
-
-
-
-
-
14
-
1
1
-
-
-
2
-
-
1
2
-
-
-
-
-
1
-
-
-
-
2
2
-
-
-
-
1
-
-
-
-
-
-
-
-
14
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
639232
Gorlatova
Purification, characterization ...
Neurospora crassa
Appl. Environ. Microbiol.
64
1029-1033
1998
-
-
-
-
-
-
8
10
-
-
2
-
-
10
-
-
2
-
-
1
1
-
20
1
1
1
-
-
9
1
-
-
2
-
-
-
-
-
-
2
-
-
-
-
15
-
10
-
-
2
-
-
-
-
2
-
1
1
-
20
1
1
-
-
9
1
-
-
-
-
-
-
-
-
-
698266
Balogh-Hergovich
Copper-mediated oxygenation of ...
Cyberlindnera mrakii
Inorg. Chem.
37
6535-6537
1998
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
697294
Balogh-Hergovich
-
Copper mediated conversion of ...
Cyberlindnera mrakii
Chem. Lett.
25
573-574
1996
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
639222
Kido
-
2-Nitropropane dioxygenase fro ...
Cyberlindnera mrakii
Agric. Biol. Chem.
48
2549-2554
1984
-
-
-
-
-
-
-
21
-
2
2
1
-
2
-
-
2
-
-
-
2
-
23
2
1
-
-
-
-
4
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
21
-
2
2
1
-
-
-
2
-
-
2
-
23
2
-
-
-
-
4
-
-
-
-
-
-
-
-
-
639226
Kido
-
Characterization of primary ni ...
Cyberlindnera mrakii
Agric. Biol. Chem.
48
1361-1362
1984
-
-
-
-
-
-
-
1
-
-
1
-
-
1
-
-
-
-
-
-
-
-
4
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
639227
Kido
Oxidation of anionic nitroalka ...
Cyberlindnera mrakii
Arch. Biochem. Biophys.
234
468-475
1984
-
-
-
-
-
-
11
2
-
1
-
-
-
9
-
-
1
1
-
-
-
-
8
-
1
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
14
-
2
-
1
-
-
-
-
-
1
-
-
-
-
8
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
639224
Kido
Properties of 2-nitropropane d ...
Cyberlindnera mrakii, Cyberlindnera mrakii IF0 0895
J. Biol. Chem.
253
226-232
1978
-
-
-
-
-
-
19
2
-
-
-
-
-
11
-
-
1
2
-
-
-
-
2
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
20
-
2
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
639225
Kido
Purification and properties of ...
Fusarium oxysporum
J. Bacteriol.
133
53-58
1978
-
-
-
-
-
-
10
6
-
-
2
-
-
4
-
-
2
-
-
1
1
1
14
1
1
2
2
6
-
1
-
1
3
-
-
-
-
-
-
3
-
-
-
-
11
-
6
-
-
2
-
-
-
-
2
-
1
1
1
14
1
2
2
6
-
1
-
1
-
-
-
-
-
-
-
639223
Kido
A new oxygenase, 2-nitropropan ...
Cyberlindnera mrakii, Cyberlindnera mrakii IF0 0895
J. Biol. Chem.
251
6994-7000
1976
3
-
-
-
-
3
13
7
-
1
4
-
-
8
-
-
1
-
-
-
-
-
17
1
1
1
1
-
-
2
2
-
2
-
-
-
3
-
-
2
-
-
3
-
18
-
7
-
1
4
-
-
-
-
1
-
-
-
-
17
1
1
1
-
-
2
2
-
-
-
-
-
-
-
-
639235
Kido
Purification and properties of ...
Cyberlindnera mrakii
J. Bacteriol.
126
1261-1265
1976
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
1
-
-
1
1
-
5
1
1
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
1
-
5
1
1
-
-
-
2
-
-
-
-
-
-
-
-
-