BRENDA - Enzyme Database
show all sequences of 1.13.12.16

A new oxygenase, 2-nitropropane dioxygenase of Hansenula mrakii. Enzymologic and spectrophotometric properties

Kido, T.; Soda, K.; Suzuki, T.; Asada, K.; J. Biol. Chem. 251, 6994-7000 (1976)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
2,2'-dipyridyl
-
Cyberlindnera mrakii
2,4,6-tripyridyl-triazine
-
Cyberlindnera mrakii
o-phenanthroline
-
Cyberlindnera mrakii
General Stability
General Stability
Organism
denaturation by sodium dithionite
Cyberlindnera mrakii
gradual and irreversible loss of activity after treatment with 1% sodium lauryl sulfate or 6 M guanidine HCl, activity is reduced to 50% of its initial activity after 50 min at 37°C, complete loss of activity after 10 h
Cyberlindnera mrakii
immediate denaturation with 8 M urea or thiourea
Cyberlindnera mrakii
Inhibitors
Inhibitors
Commentary
Organism
Structure
2-mercaptoethanol
-
Cyberlindnera mrakii
8-hydroxyquinoline
strong inhibition
Cyberlindnera mrakii
cysteine
marked decrease in enzyme activity
Cyberlindnera mrakii
GSH
marked decrease in enzyme activity
Cyberlindnera mrakii
HgCl2
moderate and potent inhibitor
Cyberlindnera mrakii
additional information
EDTA does not inhibit the enzyme significantly. Iodoacetate is almost ineffective
Cyberlindnera mrakii
N-ethylmaleimide
-
Cyberlindnera mrakii
NaHSO3
-
Cyberlindnera mrakii
NEM
-
Cyberlindnera mrakii
Nitromethane
inhibits noncompetitively
Cyberlindnera mrakii
p-chloromercuribenzoate
-
Cyberlindnera mrakii
PCMB
-
Cyberlindnera mrakii
Tiron
i.e. pyrocatechol-3,5-disulfonate disodium salt; i.e. pyrocatechol-3,5-disulfonate disodium salt, strong inhibition
Cyberlindnera mrakii
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.3
-
O2
-
Cyberlindnera mrakii
4.2
-
3-Nitro-2-butanol
neutral form of substrate
Cyberlindnera mrakii
6.8
-
nitroethane
-
Cyberlindnera mrakii
6.8
-
3-Nitro-2-pentanol
-
Cyberlindnera mrakii
21.3
-
2-Nitropropane
-
Cyberlindnera mrakii
24.3
-
nitroethane
-
Cyberlindnera mrakii
25.6
-
1-Nitropropane
-
Cyberlindnera mrakii
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe3+
contains 1 g atom of non-heme iron per mol of enzyme
Cyberlindnera mrakii
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
25000
-
1 * 25000 + 1 * 39000, SDS-PAGE
Cyberlindnera mrakii
39000
-
1 * 25000 + 1 * 39000, SDS-PAGE
Cyberlindnera mrakii
60000
-
gel filtration
Cyberlindnera mrakii
64000
-
equilibrium sedimentation
Cyberlindnera mrakii
Organism
Organism
UniProt
Commentary
Textmining
Cyberlindnera mrakii
-
-
-
Cyberlindnera mrakii
-
IF0 0895
-
Cyberlindnera mrakii IF0 0895
-
IF0 0895
-
Purification (Commentary)
Purification (Commentary)
Organism
to homogeneity
Cyberlindnera mrakii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
1-nitropropane + O2
23.4% of the activity with 2-nitropropane
639223
Cyberlindnera mrakii
propionaldehyde + HNO2
-
-
-
?
1-nitropropane + O2
23.4% of the activity with 2-nitropropane
639223
Cyberlindnera mrakii IF0 0895
propionaldehyde + HNO2
-
-
-
?
2-nitropropane + O2
-
639223
Cyberlindnera mrakii
acetone + HNO2
-
-
-
?
2-nitropropane + O2
-
639223
Cyberlindnera mrakii
acetone + HNO2
-
639223
Cyberlindnera mrakii
?
2-nitropropane + O2
-
639223
Cyberlindnera mrakii IF0 0895
acetone + HNO2
-
-
-
?
2-nitropropane + O2
-
639223
Cyberlindnera mrakii IF0 0895
acetone + HNO2
-
639223
Cyberlindnera mrakii IF0 0895
?
3-nitro-2-butanol + O2
13% of the activity with 2-nitropropane
639223
Cyberlindnera mrakii
3-hydroxy-butane-2-one + HNO2
-
-
-
?
3-nitro-2-butanol + O2
slight oxidation
639223
Cyberlindnera mrakii
3-hydroxy-butane-2-one + HNO2
-
-
-
?
3-nitro-2-pentanol + O2
40.6% of the activity with 2-nitropropane
639223
Cyberlindnera mrakii
2-hydroxy-pentane-3-one + HNO2
-
-
-
?
3-nitropropionic acid + O2
11.7% of the activity with 2-nitropropane
639223
Cyberlindnera mrakii
?
-
-
-
?
additional information
sodium dithionite also reduces both the enzyme-bound FAD and Fe3+ under anaerobic conditions
639223
Cyberlindnera mrakii
?
-
-
-
?
additional information
sodium dithionite also reduces both the enzyme-bound FAD and Fe3+ under anaerobic conditions
639223
Cyberlindnera mrakii IF0 0895
?
-
-
-
?
nitroethane + O2
88% of the activity with nitroethane
639223
Cyberlindnera mrakii
acetaldehyde + HNO2
-
-
-
?
nitroethane + O2
88% of the activity with nitroethane
639223
Cyberlindnera mrakii
acetaldehyde + HNO2
-
639223
Cyberlindnera mrakii
?
nitroethane + O2
88% of the activity with nitroethane
639223
Cyberlindnera mrakii IF0 0895
acetaldehyde + HNO2
-
-
-
?
nitromethane + O2
no activity
639223
Cyberlindnera mrakii
formaldehyde + HNO2
-
-
-
?
nitromethane + O2
is not a substrate, under anaerobic conditions. The aerobic dialysis of the enzyme treated with nitromethane causes reoxidation of only the Fe2+
639223
Cyberlindnera mrakii
formaldehyde + HNO2
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
1 * 25000 + 1 * 39000, SDS-PAGE
Cyberlindnera mrakii
Synonyms
Synonyms
Commentary
Organism
2-nitropropane dioxygenase
-
Cyberlindnera mrakii
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
40
-
-
Cyberlindnera mrakii
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
20
45
-
Cyberlindnera mrakii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
when the enzyme is dialyzed against 10 mM potassium phosphate buffer (pH 7.0) immediately after reduction by dithionite, the absorption spectrum similar to that of the native enzyme appears with concomitant restoration of approximately 80% of the activity
Cyberlindnera mrakii
8
-
-
Cyberlindnera mrakii
pH Range
pH Minimum
pH Maximum
Commentary
Organism
7
8.5
-
Cyberlindnera mrakii
7
8.5
when the enzyme is acidified to pH 3.0 and treated in the same way, the prosthetic groups do not dissociate from the protein and almost full activity remained
Cyberlindnera mrakii
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
contains 0.95 mol of FAD per mol of enzyme
Cyberlindnera mrakii
FAD
contains 0.95 mol of FAD per mol of enzyme. The enzyme-bound FAD is reduced by 2-nitropropane under anaerobic conditions
Cyberlindnera mrakii
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
2,2'-dipyridyl
-
Cyberlindnera mrakii
2,4,6-tripyridyl-triazine
-
Cyberlindnera mrakii
o-phenanthroline
-
Cyberlindnera mrakii
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
contains 0.95 mol of FAD per mol of enzyme
Cyberlindnera mrakii
FAD
contains 0.95 mol of FAD per mol of enzyme. The enzyme-bound FAD is reduced by 2-nitropropane under anaerobic conditions
Cyberlindnera mrakii
General Stability (protein specific)
General Stability
Organism
denaturation by sodium dithionite
Cyberlindnera mrakii
gradual and irreversible loss of activity after treatment with 1% sodium lauryl sulfate or 6 M guanidine HCl, activity is reduced to 50% of its initial activity after 50 min at 37°C, complete loss of activity after 10 h
Cyberlindnera mrakii
immediate denaturation with 8 M urea or thiourea
Cyberlindnera mrakii
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2-mercaptoethanol
-
Cyberlindnera mrakii
8-hydroxyquinoline
-
Cyberlindnera mrakii
8-hydroxyquinoline
strong inhibition
Cyberlindnera mrakii
cysteine
-
Cyberlindnera mrakii
cysteine
marked decrease in enzyme activity
Cyberlindnera mrakii
GSH
-
Cyberlindnera mrakii
GSH
marked decrease in enzyme activity
Cyberlindnera mrakii
HgCl2
-
Cyberlindnera mrakii
HgCl2
moderate and potent inhibitor
Cyberlindnera mrakii
additional information
EDTA does not inhibit the enzyme significantly. Iodoacetate is almost ineffective
Cyberlindnera mrakii
N-ethylmaleimide
-
Cyberlindnera mrakii
NaHSO3
-
Cyberlindnera mrakii
NEM
-
Cyberlindnera mrakii
Nitromethane
inhibits noncompetitively
Cyberlindnera mrakii
p-chloromercuribenzoate
-
Cyberlindnera mrakii
PCMB
-
Cyberlindnera mrakii
Tiron
i.e. pyrocatechol-3,5-disulfonate disodium salt
Cyberlindnera mrakii
Tiron
i.e. pyrocatechol-3,5-disulfonate disodium salt, strong inhibition
Cyberlindnera mrakii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.3
-
O2
-
Cyberlindnera mrakii
4.2
-
3-Nitro-2-butanol
neutral form of substrate
Cyberlindnera mrakii
6.8
-
nitroethane
-
Cyberlindnera mrakii
6.8
-
3-Nitro-2-pentanol
-
Cyberlindnera mrakii
21.3
-
2-Nitropropane
-
Cyberlindnera mrakii
24.3
-
nitroethane
-
Cyberlindnera mrakii
25.6
-
1-Nitropropane
-
Cyberlindnera mrakii
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe3+
contains 1 g atom of non-heme iron per mol of enzyme
Cyberlindnera mrakii
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
25000
-
1 * 25000 + 1 * 39000, SDS-PAGE
Cyberlindnera mrakii
39000
-
1 * 25000 + 1 * 39000, SDS-PAGE
Cyberlindnera mrakii
60000
-
gel filtration
Cyberlindnera mrakii
64000
-
equilibrium sedimentation
Cyberlindnera mrakii
Purification (Commentary) (protein specific)
Commentary
Organism
to homogeneity
Cyberlindnera mrakii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
1-nitropropane + O2
23.4% of the activity with 2-nitropropane
639223
Cyberlindnera mrakii
propionaldehyde + HNO2
-
-
-
?
1-nitropropane + O2
23.4% of the activity with 2-nitropropane
639223
Cyberlindnera mrakii IF0 0895
propionaldehyde + HNO2
-
-
-
?
2-nitropropane + O2
-
639223
Cyberlindnera mrakii
acetone + HNO2
-
-
-
?
2-nitropropane + O2
-
639223
Cyberlindnera mrakii
acetone + HNO2
-
639223
Cyberlindnera mrakii
?
2-nitropropane + O2
-
639223
Cyberlindnera mrakii IF0 0895
acetone + HNO2
-
-
-
?
2-nitropropane + O2
-
639223
Cyberlindnera mrakii IF0 0895
acetone + HNO2
-
639223
Cyberlindnera mrakii IF0 0895
?
3-nitro-2-butanol + O2
13% of the activity with 2-nitropropane
639223
Cyberlindnera mrakii
3-hydroxy-butane-2-one + HNO2
-
-
-
?
3-nitro-2-butanol + O2
slight oxidation
639223
Cyberlindnera mrakii
3-hydroxy-butane-2-one + HNO2
-
-
-
?
3-nitro-2-pentanol + O2
40.6% of the activity with 2-nitropropane
639223
Cyberlindnera mrakii
2-hydroxy-pentane-3-one + HNO2
-
-
-
?
3-nitropropionic acid + O2
11.7% of the activity with 2-nitropropane
639223
Cyberlindnera mrakii
?
-
-
-
?
additional information
sodium dithionite also reduces both the enzyme-bound FAD and Fe3+ under anaerobic conditions
639223
Cyberlindnera mrakii
?
-
-
-
?
additional information
sodium dithionite also reduces both the enzyme-bound FAD and Fe3+ under anaerobic conditions
639223
Cyberlindnera mrakii IF0 0895
?
-
-
-
?
nitroethane + O2
88% of the activity with nitroethane
639223
Cyberlindnera mrakii
acetaldehyde + HNO2
-
-
-
?
nitroethane + O2
88% of the activity with nitroethane
639223
Cyberlindnera mrakii
acetaldehyde + HNO2
-
639223
Cyberlindnera mrakii
?
nitroethane + O2
88% of the activity with nitroethane
639223
Cyberlindnera mrakii IF0 0895
acetaldehyde + HNO2
-
-
-
?
nitromethane + O2
no activity
639223
Cyberlindnera mrakii
formaldehyde + HNO2
-
-
-
?
nitromethane + O2
is not a substrate, under anaerobic conditions. The aerobic dialysis of the enzyme treated with nitromethane causes reoxidation of only the Fe2+
639223
Cyberlindnera mrakii
formaldehyde + HNO2
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
1 * 25000 + 1 * 39000, SDS-PAGE
Cyberlindnera mrakii
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
40
-
-
Cyberlindnera mrakii
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
20
45
-
Cyberlindnera mrakii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
when the enzyme is dialyzed against 10 mM potassium phosphate buffer (pH 7.0) immediately after reduction by dithionite, the absorption spectrum similar to that of the native enzyme appears with concomitant restoration of approximately 80% of the activity
Cyberlindnera mrakii
8
-
-
Cyberlindnera mrakii
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
7
8.5
-
Cyberlindnera mrakii
7
8.5
when the enzyme is acidified to pH 3.0 and treated in the same way, the prosthetic groups do not dissociate from the protein and almost full activity remained
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
-
-
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
-
-
-
-
-
-
-
-
-