BRENDA - Enzyme Database
show all sequences of 1.14.12.22

Purification and characterization of carbazole 1,9a-dioxygenase, a three-component dioxygenase system of Pseudomonas resinovorans strain CA10

Nam, J.-W.; Nojiri, H.; Noguchi, H.; Uchimura, H.; Yoshida, T.; Habe, H.; Yamane, H.; Omori, T.; Appl. Environ. Microbiol. 68, 5882-5890 (2002)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expression of ferredoxin subunit CarAc in Escherichia coli, His-tagged; expression of ferredoxin subunit CarAc in Escherichia coli, His-tagged; expression of terminal oxygenase CarAa in Escherichia coli in native form
Pseudomonas resinovorans
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0034
-
NADH
CarAd activity, electron acceptor 2,6-dichlorophenolindophenol, pH 7.5, 30°C
Pseudomonas resinovorans
0.182
-
NADPH
CarAd activity, electron acceptor 2,6-dichlorophenolindophenol, pH 7.5, 30°C
Pseudomonas resinovorans
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Iron
subunit CarAc, one Rieske type [2Fe-2S] cluster per monomer protein. The iron and sulfur contents of His-tagged CarAc are 1.7 to 1.9 and 1.3 to 1.6 mol/mol of protein, respectively; subunit CarAd, one Rieske type [2Fe-2S] cluster per monomer protein. The iron and sulfur contents of His-tagged CarAc are 1.8 to 2.0 and 1.8 to 1.9 mol/mol of protein, respectively; terminal oxygenase subunit contains one Rieske type [2Fe2S] cluster and one mononuclear iron center in each monomer
Pseudomonas resinovorans
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
13000
-
gel filtration
Pseudomonas resinovorans
37000
-
gel filtration
Pseudomonas resinovorans
43782
-
3 * 44000, SDS-PAGE, 3 * 43782, calculated, subunit CarAa
Pseudomonas resinovorans
44000
-
3 * 44000, SDS-PAGE, 3 * 43782, calculated, subunit CarAa
Pseudomonas resinovorans
132000
-
gel filtration, subunit CarAa
Pseudomonas resinovorans
Organism
Organism
UniProt
Commentary
Textmining
Pseudomonas resinovorans
-
-
-
Pseudomonas resinovorans
Q8GI14
ferredoxin reductase subunit CarAd
-
Pseudomonas resinovorans
Q8GI16
ferredoxin subunit CarAc
-
Pseudomonas resinovorans CA10
-
-
-
Pseudomonas resinovorans CA10
Q8GI14
ferredoxin reductase subunit CarAd
-
Pseudomonas resinovorans CA10
Q8GI16
ferredoxin subunit CarAc
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant protein; recombinant protein
Pseudomonas resinovorans
Storage Stability
Storage Stability
Organism
0°C 10% glycerol, 8 days, more than 90% residual activity, isolated subunit CarAa
Pseudomonas resinovorans
0°C 50 mM Tris-HCl pH 7.5, 24 h, 90% residual activity, reconstitued CARDO system
Pseudomonas resinovorans
0°C, 10 h, full activity, and 100 h, 93% residual activiy, ferredoxin reductase subunit CarAd
Pseudomonas resinovorans
0°C, 10% glycerol, 8 days, more than 90% residual activity for isolated subunit CarAa
Pseudomonas resinovorans
0°C, 50 mM Tris-HCl pH 7.5, 24 h, 90% residual activity for reconstituted CARDO system
Pseudomonas resinovorans
4°C, 10% glycerol, 24 h, full activity for isolated subunit CarAa
Pseudomonas resinovorans
4°C, 10% glycerol, 24 h, full activity, isolated subunit CarAa
Pseudomonas resinovorans
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
carbazole + NADH + H+ + O2
-
707219
Pseudomonas resinovorans
2'-aminobiphenyl-2,3-diol + NAD+
-
-
-
?
carbazole + NADH + H+ + O2
-
707219
Pseudomonas resinovorans CA10
2'-aminobiphenyl-2,3-diol + NAD+
-
-
-
?
carbazole + NADPH + H+ + O2
-
707219
Pseudomonas resinovorans
2'-aminobiphenyl-2,3-diol + NADP+
-
-
-
?
carbazole + NADPH + H+ + O2
-
707219
Pseudomonas resinovorans CA10
2'-aminobiphenyl-2,3-diol + NADP+
-
-
-
?
additional information
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. Terminal oxygenase subunit CarAa is reduced by His-tagged CarAc, His-tagged CarAd, and NADH. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
707219
Pseudomonas resinovorans
?
-
-
-
-
additional information
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
707219
Pseudomonas resinovorans
?
-
-
-
-
additional information
terminal oxygenase subunit CarAa is reduced by His-tagged ferredoxin CarAc, His-tagged ferredoxin reductase CarAd, and NADH. The three purified proteins can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
707219
Pseudomonas resinovorans
?
-
-
-
-
additional information
terminal oxygenase subunit CarAa is reduced by His-tagged ferredoxin CarAc, His-tagged ferredoxin reductase CarAd, and NADH. The three purified proteins can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
707219
Pseudomonas resinovorans CA10
?
-
-
-
-
additional information
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. Terminal oxygenase subunit CarAa is reduced by His-tagged CarAc, His-tagged CarAd, and NADH. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
707219
Pseudomonas resinovorans CA10
?
-
-
-
-
additional information
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
707219
Pseudomonas resinovorans CA10
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
monomer
1 * 13000, SDS-PAGE, subunit CarAc; 1 * 37000, SDS-PAGE, subunit CarAd
Pseudomonas resinovorans
trimer
3 * 44000, SDS-PAGE, 3 * 43782, calculated, subunit CarAa
Pseudomonas resinovorans
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
;
Pseudomonas resinovorans
35
45
maximum cytochrome c reductase activity of subunit CarAd
Pseudomonas resinovorans
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
8.5
maximum cytochrome c reductase activity of subunit CarAd
Pseudomonas resinovorans
7.5
-
;
Pseudomonas resinovorans
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
1 mol of His-tagged CarAd contains 1 mol of FAD
Pseudomonas resinovorans
NADH
both NADH and NADPH are effective as electron donors for His-tagged ferrdoxin reductase CarAd. The ratio kcat/Km for NADH is 22.3-fold higher than that for NADPH in the 2,6-dichlorophenolindophenol reductase assay
Pseudomonas resinovorans
NADPH
both NADH and NADPH are effective as electron donors for His-tagged ferrdoxin reductase CarAd. The ratio kcat/Km for NADH is 22.3-fold higher than that for NADPH in the 2,6-dichlorophenolindophenol reductase assay
Pseudomonas resinovorans
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of ferredoxin subunit CarAc in Escherichia coli, His-tagged
Pseudomonas resinovorans
expression of terminal oxygenase CarAa in Escherichia coli in native form
Pseudomonas resinovorans
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
1 mol of His-tagged CarAd contains 1 mol of FAD
Pseudomonas resinovorans
NADH
both NADH and NADPH are effective as electron donors for His-tagged ferrdoxin reductase CarAd. The ratio kcat/Km for NADH is 22.3-fold higher than that for NADPH in the 2,6-dichlorophenolindophenol reductase assay
Pseudomonas resinovorans
NADPH
both NADH and NADPH are effective as electron donors for His-tagged ferrdoxin reductase CarAd. The ratio kcat/Km for NADH is 22.3-fold higher than that for NADPH in the 2,6-dichlorophenolindophenol reductase assay
Pseudomonas resinovorans
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0034
-
NADH
CarAd activity, electron acceptor 2,6-dichlorophenolindophenol, pH 7.5, 30°C
Pseudomonas resinovorans
0.182
-
NADPH
CarAd activity, electron acceptor 2,6-dichlorophenolindophenol, pH 7.5, 30°C
Pseudomonas resinovorans
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Iron
terminal oxygenase subunit contains one Rieske type [2Fe2S] cluster and one mononuclear iron center in each monomer
Pseudomonas resinovorans
Iron
subunit CarAc, one Rieske type [2Fe-2S] cluster per monomer protein. The iron and sulfur contents of His-tagged CarAc are 1.7 to 1.9 and 1.3 to 1.6 mol/mol of protein, respectively
Pseudomonas resinovorans
Iron
subunit CarAd, one Rieske type [2Fe-2S] cluster per monomer protein. The iron and sulfur contents of His-tagged CarAc are 1.8 to 2.0 and 1.8 to 1.9 mol/mol of protein, respectively
Pseudomonas resinovorans
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
13000
-
gel filtration
Pseudomonas resinovorans
37000
-
gel filtration
Pseudomonas resinovorans
43782
-
3 * 44000, SDS-PAGE, 3 * 43782, calculated, subunit CarAa
Pseudomonas resinovorans
44000
-
3 * 44000, SDS-PAGE, 3 * 43782, calculated, subunit CarAa
Pseudomonas resinovorans
132000
-
gel filtration, subunit CarAa
Pseudomonas resinovorans
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant protein
Pseudomonas resinovorans
Storage Stability (protein specific)
Storage Stability
Organism
0°C 10% glycerol, 8 days, more than 90% residual activity, isolated subunit CarAa
Pseudomonas resinovorans
0°C 50 mM Tris-HCl pH 7.5, 24 h, 90% residual activity, reconstitued CARDO system
Pseudomonas resinovorans
0°C, 10 h, full activity, and 100 h, 93% residual activiy, ferredoxin reductase subunit CarAd
Pseudomonas resinovorans
0°C, 10% glycerol, 8 days, more than 90% residual activity for isolated subunit CarAa
Pseudomonas resinovorans
0°C, 50 mM Tris-HCl pH 7.5, 24 h, 90% residual activity for reconstituted CARDO system
Pseudomonas resinovorans
4°C, 10% glycerol, 24 h, full activity for isolated subunit CarAa
Pseudomonas resinovorans
4°C, 10% glycerol, 24 h, full activity, isolated subunit CarAa
Pseudomonas resinovorans
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
carbazole + NADH + H+ + O2
-
707219
Pseudomonas resinovorans
2'-aminobiphenyl-2,3-diol + NAD+
-
-
-
?
carbazole + NADH + H+ + O2
-
707219
Pseudomonas resinovorans CA10
2'-aminobiphenyl-2,3-diol + NAD+
-
-
-
?
carbazole + NADPH + H+ + O2
-
707219
Pseudomonas resinovorans
2'-aminobiphenyl-2,3-diol + NADP+
-
-
-
?
carbazole + NADPH + H+ + O2
-
707219
Pseudomonas resinovorans CA10
2'-aminobiphenyl-2,3-diol + NADP+
-
-
-
?
additional information
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. Terminal oxygenase subunit CarAa is reduced by His-tagged CarAc, His-tagged CarAd, and NADH. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
707219
Pseudomonas resinovorans
?
-
-
-
-
additional information
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
707219
Pseudomonas resinovorans
?
-
-
-
-
additional information
terminal oxygenase subunit CarAa is reduced by His-tagged ferredoxin CarAc, His-tagged ferredoxin reductase CarAd, and NADH. The three purified proteins can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
707219
Pseudomonas resinovorans
?
-
-
-
-
additional information
terminal oxygenase subunit CarAa is reduced by His-tagged ferredoxin CarAc, His-tagged ferredoxin reductase CarAd, and NADH. The three purified proteins can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
707219
Pseudomonas resinovorans CA10
?
-
-
-
-
additional information
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. Terminal oxygenase subunit CarAa is reduced by His-tagged CarAc, His-tagged CarAd, and NADH. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
707219
Pseudomonas resinovorans CA10
?
-
-
-
-
additional information
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
707219
Pseudomonas resinovorans CA10
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 13000, SDS-PAGE, subunit CarAc
Pseudomonas resinovorans
monomer
1 * 37000, SDS-PAGE, subunit CarAd
Pseudomonas resinovorans
trimer
3 * 44000, SDS-PAGE, 3 * 43782, calculated, subunit CarAa
Pseudomonas resinovorans
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
-
Pseudomonas resinovorans
35
45
maximum cytochrome c reductase activity of subunit CarAd
Pseudomonas resinovorans
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
8.5
maximum cytochrome c reductase activity of subunit CarAd
Pseudomonas resinovorans
7.5
-
-
Pseudomonas resinovorans
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
130
-
NADPH
CarAd activity, electron acceptor 2,6-dichlorophenolindophenol, pH 7.5, 30°C
Pseudomonas resinovorans
2900
-
NADH
CarAd activity, electron acceptor 2,6-dichlorophenolindophenol, pH 7.5, 30°C
Pseudomonas resinovorans
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
130
-
NADPH
CarAd activity, electron acceptor 2,6-dichlorophenolindophenol, pH 7.5, 30°C
Pseudomonas resinovorans
2900
-
NADH
CarAd activity, electron acceptor 2,6-dichlorophenolindophenol, pH 7.5, 30°C
Pseudomonas resinovorans
Other publictions for EC 1.14.12.22
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)
742172
Khan
High-level expression, purifi ...
Pseudomonas sp. GBS.5
Biotechnol. Lett.
37
1945-1952
2015
1
-
1
-
-
-
-
-
-
-
-
2
-
2
-
-
1
-
-
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8
-
3
-
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2
-
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1
-
1
2
-
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2
-
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1
-
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8
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
742964
Ahmad
-
Substrate specificity of angu ...
Neptuniibacter sp. CAR-SF
J. Chem. Pharm. Sci.
8
382-388
2015
-
-
-
-
-
-
-
-
-
-
-
2
-
1
-
-
-
-
-
-
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8
-
1
-
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-
-
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2
-
-
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-
-
2
-
-
-
-
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2
-
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8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
741525
Matsuzawa
Crystallization and prelimina ...
Janthinobacterium sp. J3
Acta crystallogr. Sect. F
70
1406-1409
2014
-
-
1
1
-
-
-
-
-
-
-
2
-
1
-
-
1
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
1
-
-
-
-
-
-
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-
-
2
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
741682
Inoue
Structural basis of the diver ...
Janthinobacterium sp. J3
Appl. Environ. Microbiol.
80
2821-2832
2014
-
-
1
1
3
-
-
3
-
-
-
2
-
3
-
-
1
-
-
-
-
-
8
-
1
-
-
-
3
-
-
-
3
-
-
-
-
-
1
3
1
3
-
-
-
-
3
-
-
-
2
-
-
-
1
-
-
-
-
8
-
-
-
-
3
-
-
-
-
-
-
-
-
3
3
724678
Ashikawa
Structural insight into the su ...
Janthinobacterium sp.
BMC Struct. Biol.
12
15
2012
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
725637
Larentis
Influence of induction conditi ...
Pseudomonas stutzeri
J. Ind. Microbiol. Biotechnol.
38
1045-1054
2011
-
-
1
-
1
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
706986
Umeda
Crystallization and preliminar ...
Sphingomonas sp., Sphingomonas sp. KA1
Acta Crystallogr. Sect. F
66
1480-1483
2010
-
-
1
1
-
-
-
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
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-
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-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
706994
Umeda
Crystallization and preliminar ...
Sphingomonas sp., Sphingomonas sp. KA1
Acta Crystallogr. Sect. F
66
712-714
2010
-
-
1
1
-
-
-
-
-
-
1
-
-
5
-
-
1
-
-
-
-
-
-
-
1
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707821
Maeda
Isolation and characterization ...
Kordiimonas gwangyangensis
Biotechnol. Lett.
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2010
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7
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710385
Gai
The genes coding for the conve ...
Sphingomonas sp., Sphingomonas sp. XLDN2-5
PLoS One
5
e10018
2010
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2
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4
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1
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2
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709526
Inoue
Specific Interactions between ...
Janthinobacterium sp. J3, Nocardioides aromaticivorans, Nocardioides aromaticivorans IC177, Pseudomonas resinovorans, Pseudomonas resinovorans CA10, Sphingomonas sp., Sphingomonas sp. KA1
J. Mol. Biol.
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2009
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4
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707776
Uchimura
Alteration of the substrate sp ...
Janthinobacterium sp. J3
Biosci. Biotechnol. Biochem.
72
3237-3248
2008
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1
17
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2
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6
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1
17
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6
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706958
Ashikawa
Crystallization and preliminar ...
Janthinobacterium sp. J3
Acta Crystallogr. Sect. F
63
499-502
2007
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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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1
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706956
Inoue
Crystallization and preliminar ...
Nocardioides aromaticivorans, Nocardioides aromaticivorans IC177
Acta Crystallogr. Sect. F
62
1212-1214
2006
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1
1
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4
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5
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1
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2
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707220
Yu
Selective biodegradation of S ...
Pseudomonas sp., Pseudomonas sp. CA10
Appl. Environ. Microbiol.
72
2235-2238
2006
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1
1
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4
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4
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1
1
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4
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710576
Ashikawa
Electron transfer complex form ...
Janthinobacterium sp. J3, Pseudomonas resinovorans, Pseudomonas resinovorans CA10
Structure
14
1779-1789
2006
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2
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1
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10
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709513
Nojiri
Structure of the terminal oxyg ...
Janthinobacterium sp. J3
J. Mol. Biol.
351
355-370
2005
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1
1
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4
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710504
Nam
Crystal structure of the ferre ...
Pseudomonas resinovorans, Pseudomonas resinovorans CA10
Proteins
58
779-789
2005
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1
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13
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707774
Saiki
Rhizoremediation of dioxin-lik ...
Sphingomonas sp., Sphingomonas sp. KA1
Biosci. Biotechnol. Biochem.
67
1144-1148
2003
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1
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1
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8
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707219
Nam
Purification and characterizat ...
Pseudomonas resinovorans, Pseudomonas resinovorans CA10
Appl. Environ. Microbiol.
68
5882-5890
2002
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1
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2
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1
5
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16
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1
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7
10
2
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2
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2
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3
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3
3
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2
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3
5
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2
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7
10
3
3
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3
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2
2
707814
Takagi
-
Detailed comparison between th ...
Pseudomonas resinovorans
Biotechnol. Lett.
24
2099-2106
2002
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1
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7
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1
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1
1
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7
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708910
Nojiri
Diverse oxygenations catalyzed ...
Pseudomonas sp., Pseudomonas sp. CA10
J. Bacteriol.
181
3105-3113
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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708908
Sato
Identification and characteriz ...
Pseudomonas sp., Pseudomonas sp. CA10
J. Bacteriol.
179
4850-4858
1997
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6
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21
1
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1
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1
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1
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21
1
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