BRENDA - Enzyme Database show
show all sequences of 1.14.12.22

Specific Interactions between the ferredoxin and terminal oxygenase components of a class IIB Rieske nonheme iron oxygenase, carbazole 1,9a-dioxygenase

Inoue, K.; Ashikawa, Y.; Umeda, T.; Abo, M.; Katsuki, J.; Usami, Y.; Noguchi, H.; Fujimoto, Z.; Terada, T.; Yamane, H.; Nojiri, H.; J. Mol. Biol. 392, 436-451 (2009)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
comparison of crystal structures of the oxygenase and ferredoxin components to the CARDOs from Pseudomonas resinovorans CA10, Janthinobacterium sp. J3, Novosphingobium sp. KA1, and Nocardioides aromaticivorans IC177 which are grouped into classes III, III, IIA, and IIB, respectively. The comparison suggests residues in common between class IIB and class III CARDOs that are important for interactions between ferredoxin and oxygenase. In the class IIB CARDOs, these include His75 and Glu71 in ferredoxin and Lys20 and Glu357 in the oxygenase for electrostatic interactions, and Phe74 and Pro90 in ferredoxin and Trp21, Leu359, and Val367 in the oxygenase for hydrophobic interactions
Janthinobacterium sp. J3
comparison of crystal structures of the oxygenase and ferredoxin components to the CARDOs from Pseudomonas resinovorans CA10, Janthinobacterium sp. J3, Novosphingobium sp. KA1, and Nocardioides aromaticivorans IC177 which are grouped into classes III, III, IIA, and IIB, respectively. The comparison suggests residues in common between class IIB and class III CARDOs that are important for interactions between ferredoxin and oxygenase. In the class IIB CARDOs, these include His75 and Glu71 in ferredoxin and Lys20 and Glu357 in the oxygenase for electrostatic interactions, and Phe74 and Pro90 in ferredoxin and Trp21, Leu359, and Val367 in the oxygenase for hydrophobic interactions
Nocardioides aromaticivorans
comparison of crystal structures of the oxygenase and ferredoxin components to the CARDOs from Pseudomonas resinovorans CA10, Janthinobacterium sp. J3, Novosphingobium sp. KA1, and Nocardioides aromaticivorans IC177 which are grouped into classes III, III, IIA, and IIB, respectively. The comparison suggests residues in common between class IIB and class III CARDOs that are important for interactions between ferredoxin and oxygenase. In the class IIB CARDOs, these include His75 and Glu71 in ferredoxin and Lys20 and Glu357 in the oxygenase for electrostatic interactions, and Phe74 and Pro90 in ferredoxin and Trp21, Leu359, and Val367 in the oxygenase for hydrophobic interactions
Pseudomonas resinovorans
comparison of crystal structures of the oxygenase and ferredoxin components to the CARDOs from Pseudomonas resinovorans CA10, Janthinobacterium sp. J3, Novosphingobium sp. KA1, and Nocardioides aromaticivorans IC177 which are grouped into classes III, III, IIA, and IIB, respectively. The comparison suggests residues in common between class IIB and class III CARDOs that are important for interactions between ferredoxin and oxygenase. In the class IIB CARDOs, these include His75 and Glu71 in ferredoxin and Lys20 and Glu357 in the oxygenase for electrostatic interactions, and Phe74 and Pro90 in ferredoxin and Trp21, Leu359, and Val367 in the oxygenase for hydrophobic interactions
Sphingomonas sp.
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Janthinobacterium sp. J3
-
-
-
Nocardioides aromaticivorans
-
-
-
Nocardioides aromaticivorans IC177
-
-
-
Pseudomonas resinovorans
-
-
-
Pseudomonas resinovorans CA10
-
-
-
Sphingomonas sp.
-
-
-
Sphingomonas sp. KA1
-
-
-
Purification (Commentary)
Commentary
Organism
-
Nocardioides aromaticivorans
Crystallization (Commentary) (protein specific)
Crystallization
Organism
comparison of crystal structures of the oxygenase and ferredoxin components to the CARDOs from Pseudomonas resinovorans CA10, Janthinobacterium sp. J3, Novosphingobium sp. KA1, and Nocardioides aromaticivorans IC177 which are grouped into classes III, III, IIA, and IIB, respectively. The comparison suggests residues in common between class IIB and class III CARDOs that are important for interactions between ferredoxin and oxygenase. In the class IIB CARDOs, these include His75 and Glu71 in ferredoxin and Lys20 and Glu357 in the oxygenase for electrostatic interactions, and Phe74 and Pro90 in ferredoxin and Trp21, Leu359, and Val367 in the oxygenase for hydrophobic interactions
Janthinobacterium sp. J3
comparison of crystal structures of the oxygenase and ferredoxin components to the CARDOs from Pseudomonas resinovorans CA10, Janthinobacterium sp. J3, Novosphingobium sp. KA1, and Nocardioides aromaticivorans IC177 which are grouped into classes III, III, IIA, and IIB, respectively. The comparison suggests residues in common between class IIB and class III CARDOs that are important for interactions between ferredoxin and oxygenase. In the class IIB CARDOs, these include His75 and Glu71 in ferredoxin and Lys20 and Glu357 in the oxygenase for electrostatic interactions, and Phe74 and Pro90 in ferredoxin and Trp21, Leu359, and Val367 in the oxygenase for hydrophobic interactions
Nocardioides aromaticivorans
comparison of crystal structures of the oxygenase and ferredoxin components to the CARDOs from Pseudomonas resinovorans CA10, Janthinobacterium sp. J3, Novosphingobium sp. KA1, and Nocardioides aromaticivorans IC177 which are grouped into classes III, III, IIA, and IIB, respectively. The comparison suggests residues in common between class IIB and class III CARDOs that are important for interactions between ferredoxin and oxygenase. In the class IIB CARDOs, these include His75 and Glu71 in ferredoxin and Lys20 and Glu357 in the oxygenase for electrostatic interactions, and Phe74 and Pro90 in ferredoxin and Trp21, Leu359, and Val367 in the oxygenase for hydrophobic interactions
Pseudomonas resinovorans
comparison of crystal structures of the oxygenase and ferredoxin components to the CARDOs from Pseudomonas resinovorans CA10, Janthinobacterium sp. J3, Novosphingobium sp. KA1, and Nocardioides aromaticivorans IC177 which are grouped into classes III, III, IIA, and IIB, respectively. The comparison suggests residues in common between class IIB and class III CARDOs that are important for interactions between ferredoxin and oxygenase. In the class IIB CARDOs, these include His75 and Glu71 in ferredoxin and Lys20 and Glu357 in the oxygenase for electrostatic interactions, and Phe74 and Pro90 in ferredoxin and Trp21, Leu359, and Val367 in the oxygenase for hydrophobic interactions
Sphingomonas sp.
Purification (Commentary) (protein specific)
Commentary
Organism
-
Nocardioides aromaticivorans
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
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
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37
1945-1952
2015
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742964
Ahmad
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Substrate specificity of angu ...
Neptuniibacter sp. CAR-SF
J. Chem. Pharm. Sci.
8
382-388
2015
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741525
Matsuzawa
Crystallization and prelimina ...
Janthinobacterium sp. J3
Acta crystallogr. Sect. F
70
1406-1409
2014
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1
1
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2
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741682
Inoue
Structural basis of the diver ...
Janthinobacterium sp. J3
Appl. Environ. Microbiol.
80
2821-2832
2014
-
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1
1
3
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3
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2
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3
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1
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8
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3
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3
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1
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1
3
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3
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1
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8
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3
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3
3
724678
Ashikawa
Structural insight into the su ...
Janthinobacterium sp.
BMC Struct. Biol.
12
15
2012
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1
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1
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725637
Larentis
Influence of induction conditi ...
Pseudomonas stutzeri
J. Ind. Microbiol. Biotechnol.
38
1045-1054
2011
-
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1
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1
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4
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1
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706986
Umeda
Crystallization and preliminar ...
Sphingomonas sp., Sphingomonas sp. KA1
Acta Crystallogr. Sect. F
66
1480-1483
2010
-
-
1
1
-
-
-
-
-
-
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-
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3
-
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1
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706994
Umeda
Crystallization and preliminar ...
Sphingomonas sp., Sphingomonas sp. KA1
Acta Crystallogr. Sect. F
66
712-714
2010
-
-
1
1
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1
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5
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1
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707821
Maeda
Isolation and characterization ...
Kordiimonas gwangyangensis
Biotechnol. Lett.
32
1725-1731
2010
-
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1
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3
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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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-
-
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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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1
-
-
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-
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10
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4
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1
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2
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.
392
436-451
2009
-
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4
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17
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1
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4
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1
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-
-
-
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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
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1
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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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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2
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707220
Yu
Selective biodegradation of S ...
Pseudomonas sp., Pseudomonas sp. CA10
Appl. Environ. Microbiol.
72
2235-2238
2006
-
1
1
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4
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4
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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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12
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1
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1
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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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1
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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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15
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1
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7
10
2
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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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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4
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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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5
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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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