BRENDA - Enzyme Database
show all sequences of 1.13.12.16

Oxidation of alkyl nitronates catalyzed by 2-nitropropane dioxygenase from Hansenula mrakii

Mijatovic, S.; Gadda, G.; Arch. Biochem. Biophys. 473, 61-68 (2008)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expressed in Escherichia coli
Cyberlindnera mrakii
Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
superoxide dismutase and catalase have no effect on the enzymatic activity
Cyberlindnera mrakii
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
the enzyme contains negligible amounts of iron, manganese, zinc, and copper ions, which are not catalytically relevant
Cyberlindnera mrakii
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
SDS-PAGE
Cyberlindnera mrakii
Organism
Organism
UniProt
Commentary
Textmining
Cyberlindnera mrakii
Q12723
-
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Cyberlindnera mrakii
Source Tissue
Source Tissue
Commentary
Organism
Textmining
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
butyl-1-nitronate + O2
-
684712
Cyberlindnera mrakii
NO2- + butanal
-
-
-
?
ethylnitronate + O2
-
684712
Cyberlindnera mrakii
NO2- + acetaldehyde
-
-
-
?
hexyl-1-nitronate + O2
-
684712
Cyberlindnera mrakii
NO2- + hexanal
-
-
-
?
additional information
anaerobic substrate reduction and kinetic data using a Clark oxygen electrode to measure rates of oxygen consumption indicated that the enzyme is active on a broad range of alkyl nitronates, with a marked preference for unbranched substrates over propyl-2-nitronate. The enzyme utilizes alkyl nitronates for catalysis, but not nitroalkanes
684712
Cyberlindnera mrakii
?
-
-
-
?
additional information
anaerobic substrate reduction and kinetic data using a Clark oxygen electrode to measure rates of oxygen consumption indicates that the enzyme is active on a broad range of alkyl nitronates, with a marked preference for unbranched substrates over propyl-2-nitronate. The enzyme utilizes alkyl nitronates for catalysis, but not nitroalkanes
684712
Cyberlindnera mrakii
?
-
-
-
?
pentyl-1-nitronate + O2
-
684712
Cyberlindnera mrakii
NO2- + pentanal
-
-
-
?
propyl-1-nitronate + O2
-
684712
Cyberlindnera mrakii
NO2- + propionaldehyde
-
-
-
?
propyl-2-nitronate + O2
-
684712
Cyberlindnera mrakii
NO2- + acetone
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
2-nitropropane dioxygenase
-
Cyberlindnera mrakii
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Cyberlindnera mrakii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
assay at
Cyberlindnera mrakii
8
-
assay at
Cyberlindnera mrakii
Cofactor
Cofactor
Commentary
Organism
Structure
FMN
present in a 1:1 stoichiometry with the protein. The tight binding of sulfite (Kd = 0.09 mM, at pH 8 and 15°C) to the enzyme and the formation of the anionic flavosemiquinone upon anaerobic incubation with alkyl nitronates are consistent with the presence of a positively charged group in proximity of the N(1)-C(2)=O atoms of the FMN cofactor
Cyberlindnera mrakii
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli
Cyberlindnera mrakii
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FMN
present in a 1:1 stoichiometry with the protein. The tight binding of sulfite (Kd = 0.09 mM, at pH 8 and 15°C) to the enzyme and the formation of the anionic flavosemiquinone upon anaerobic incubation with alkyl nitronates are consistent with the presence of a positively charged group in proximity of the N(1)-C(2)=O atoms of the FMN cofactor
Cyberlindnera mrakii
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
additional information
superoxide dismutase and catalase have no effect on the enzymatic activity
Cyberlindnera mrakii
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
the enzyme contains negligible amounts of iron, manganese, zinc, and copper ions, which are not catalytically relevant
Cyberlindnera mrakii
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
SDS-PAGE
Cyberlindnera mrakii
Purification (Commentary) (protein specific)
Commentary
Organism
-
Cyberlindnera mrakii
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
butyl-1-nitronate + O2
-
684712
Cyberlindnera mrakii
NO2- + butanal
-
-
-
?
ethylnitronate + O2
-
684712
Cyberlindnera mrakii
NO2- + acetaldehyde
-
-
-
?
hexyl-1-nitronate + O2
-
684712
Cyberlindnera mrakii
NO2- + hexanal
-
-
-
?
additional information
anaerobic substrate reduction and kinetic data using a Clark oxygen electrode to measure rates of oxygen consumption indicated that the enzyme is active on a broad range of alkyl nitronates, with a marked preference for unbranched substrates over propyl-2-nitronate. The enzyme utilizes alkyl nitronates for catalysis, but not nitroalkanes
684712
Cyberlindnera mrakii
?
-
-
-
?
additional information
anaerobic substrate reduction and kinetic data using a Clark oxygen electrode to measure rates of oxygen consumption indicates that the enzyme is active on a broad range of alkyl nitronates, with a marked preference for unbranched substrates over propyl-2-nitronate. The enzyme utilizes alkyl nitronates for catalysis, but not nitroalkanes
684712
Cyberlindnera mrakii
?
-
-
-
?
pentyl-1-nitronate + O2
-
684712
Cyberlindnera mrakii
NO2- + pentanal
-
-
-
?
propyl-1-nitronate + O2
-
684712
Cyberlindnera mrakii
NO2- + propionaldehyde
-
-
-
?
propyl-2-nitronate + O2
-
684712
Cyberlindnera mrakii
NO2- + acetone
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Cyberlindnera mrakii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
assay at
Cyberlindnera mrakii
8
-
assay at
Cyberlindnera mrakii
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1.6
-
propyl-2-nitronate
-
Cyberlindnera mrakii
112
-
butyl-1-nitronate
-
Cyberlindnera mrakii
121
-
pentyl-1-nitronate
-
Cyberlindnera mrakii
129
-
ethylnitronate
-
Cyberlindnera mrakii
130
-
hexyl-1-nitronate
-
Cyberlindnera mrakii
170
-
propyl-1-nitronate
-
Cyberlindnera mrakii
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1.6
-
propyl-2-nitronate
-
Cyberlindnera mrakii
112
-
butyl-1-nitronate
-
Cyberlindnera mrakii
121
-
pentyl-1-nitronate
-
Cyberlindnera mrakii
129
-
ethylnitronate
-
Cyberlindnera mrakii
130
-
hexyl-1-nitronate
-
Cyberlindnera mrakii
170
-
propyl-1-nitronate
-
Cyberlindnera mrakii
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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1
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3
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1
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5
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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
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1
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1
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1
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1
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8
1
1
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3
1
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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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6
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3
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1
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6
6
728077
Klinkenberg
Rv1894c is a novel hypoxia-ind ...
Mycobacterium tuberculosis
J. Infect. Dis.
207
1525-1534
2013
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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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10
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3
2
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3
3
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3
3
724175
Li
Crystal structure and site-dir ...
Streptomyces ansochromogenes
Biochem. Biophys. Res. Commun.
405
344-348
2011
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1
1
3
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3
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3
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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
-
-
-
-
-
-
-
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
-
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-
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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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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2
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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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1
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1
1
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2
1
1
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2
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1
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2
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1
2
6
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1
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5
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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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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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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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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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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
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2
4
1
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7
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3
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33
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2
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28
2
1
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3
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3
3
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11
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1
33
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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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14
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1
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14
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2
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639232
Gorlatova
Purification, characterization ...
Neurospora crassa
Appl. Environ. Microbiol.
64
1029-1033
1998
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8
10
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2
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10
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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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698266
Balogh-Hergovich
Copper-mediated oxygenation of ...
Cyberlindnera mrakii
Inorg. Chem.
37
6535-6537
1998
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1
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697294
Balogh-Hergovich
-
Copper mediated conversion of ...
Cyberlindnera mrakii
Chem. Lett.
25
573-574
1996
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-
-
-
-
-
-
-
-
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
-
-
-
-
-
-
-
-
-