BRENDA - Enzyme Database show
show all sequences of 1.7.2.3

Molecular analysis of the trimethylamine N-oxide (TMAO) reductase respiratory system from a Shewanella species

Dos Santos, J.; Iobbi-Nivol, C.; Couillault, C; Giordano, G.; Mejean, V.; J. Mol. Biol. 284, 421-433 (1998)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
amplification of the structural torA gene encoding the enzyme and iits flanking regions using PCR techniques, the torA gene is the third gene of a TMAO-inducible operon, torECAD, encoding the TMAO respiratory components, the torC gene encodes a pentahemic c-type cytochrome, likely to be involved in electron transfer to the TorA terminal reductase, the role of the torE gene is unknown, torD gene encodes the TorD protein, a cytoplasmic protein involved in the folding process of the TorA precursor protein
Shewanella massilia
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.017
-
Trimethylamine N-oxide
-
Shewanella massilia
0.022
-
4-methylmorpholine N-oxide
-
Shewanella massilia
0.61
-
alpha-picoline N-oxide
-
Shewanella massilia
1
-
N,N-dimethyldodecylamine N-oxide
-
Shewanella massilia
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
periplasm
-
Shewanella massilia
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Molybdenum
-
Shewanella massilia
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
90000
-
1 * 90000, SDS-PAGE
Shewanella massilia
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
trimethylamine-N-oxide + electron donor
Shewanella massilia
-
trimethylamine + oxidized electron donor + H2O
-
Shewanella massilia
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Shewanella massilia
O87948
-
-
Purification (Commentary)
Commentary
Organism
using ion exchange chromatography on DE52 column, chromatography on a Mono Q HR 16/10 column and preparative electrophoresis
Shewanella massilia
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Shewanella massilia
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4-methylmorpholine N-oxide + electron donor
-
392775
Shewanella massilia
4-methylmorpholine + oxidized electron donor + H2O
-
392775
Shewanella massilia
?
alpha-picoline N-oxide + electron donor
alpha-picoline N-oxide is not an efficient substrate for the enzyme
392775
Shewanella massilia
alpha-picoline + H2O + oxidized electron donor
-
392775
Shewanella massilia
?
dimethylsulfoxide + electron donor
-
392775
Shewanella massilia
? + oxidized electron donor + H2O
-
392775
Shewanella massilia
?
diphenylsulfoxide + electron donor
-
392775
Shewanella massilia
diphenylsulfide + oxidized electron donor + H2O
-
-
-
-
L-methionine sulfoxide + electron donor
-
392775
Shewanella massilia
L-methionine + oxidized electron donor + H2O
-
392775
Shewanella massilia
?
N,N-dimethyldodecylamine N-oxide + electron donor
N,N-dimethyldodecylamine N-oxide is not an efficient substrate for the enzyme
392775
Shewanella massilia
N,N-dimethyldodecylamine + H2O + oxidized electron donor
-
392775
Shewanella massilia
?
trimethylamine N-oxide + electron donor
-
392775
Shewanella massilia
trimethylamine + oxidized electron donor + H2O
-
392775
Shewanella massilia
?
trimethylamine-N-oxide + electron donor
-
392775
Shewanella massilia
trimethylamine + oxidized electron donor + H2O
-
392775
Shewanella massilia
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 90000, SDS-PAGE
Shewanella massilia
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4
-
dibutylsulfoxide
value below
Shewanella massilia
4
-
Dimethylsulfoxide
value below
Shewanella massilia
4
-
diphenylsulfoxide
value below
Shewanella massilia
4
-
DL-methioninesulfoxide
value below
Shewanella massilia
78
-
alpha-picoline N-oxide
-
Shewanella massilia
109
-
4-methylmorpholine N-oxide
-
Shewanella massilia
120
-
Trimethylamine N-oxide
-
Shewanella massilia
151
-
N,N-dimethyldodecylamine N-oxide
-
Shewanella massilia
Cloned(Commentary) (protein specific)
Commentary
Organism
amplification of the structural torA gene encoding the enzyme and iits flanking regions using PCR techniques, the torA gene is the third gene of a TMAO-inducible operon, torECAD, encoding the TMAO respiratory components, the torC gene encodes a pentahemic c-type cytochrome, likely to be involved in electron transfer to the TorA terminal reductase, the role of the torE gene is unknown, torD gene encodes the TorD protein, a cytoplasmic protein involved in the folding process of the TorA precursor protein
Shewanella massilia
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.017
-
Trimethylamine N-oxide
-
Shewanella massilia
0.022
-
4-methylmorpholine N-oxide
-
Shewanella massilia
0.61
-
alpha-picoline N-oxide
-
Shewanella massilia
1
-
N,N-dimethyldodecylamine N-oxide
-
Shewanella massilia
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
periplasm
-
Shewanella massilia
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Molybdenum
-
Shewanella massilia
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
90000
-
1 * 90000, SDS-PAGE
Shewanella massilia
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
trimethylamine-N-oxide + electron donor
Shewanella massilia
-
trimethylamine + oxidized electron donor + H2O
-
Shewanella massilia
?
Purification (Commentary) (protein specific)
Commentary
Organism
using ion exchange chromatography on DE52 column, chromatography on a Mono Q HR 16/10 column and preparative electrophoresis
Shewanella massilia
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Shewanella massilia
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4-methylmorpholine N-oxide + electron donor
-
392775
Shewanella massilia
4-methylmorpholine + oxidized electron donor + H2O
-
392775
Shewanella massilia
?
alpha-picoline N-oxide + electron donor
alpha-picoline N-oxide is not an efficient substrate for the enzyme
392775
Shewanella massilia
alpha-picoline + H2O + oxidized electron donor
-
392775
Shewanella massilia
?
dimethylsulfoxide + electron donor
-
392775
Shewanella massilia
? + oxidized electron donor + H2O
-
392775
Shewanella massilia
?
diphenylsulfoxide + electron donor
-
392775
Shewanella massilia
diphenylsulfide + oxidized electron donor + H2O
-
-
-
-
L-methionine sulfoxide + electron donor
-
392775
Shewanella massilia
L-methionine + oxidized electron donor + H2O
-
392775
Shewanella massilia
?
N,N-dimethyldodecylamine N-oxide + electron donor
N,N-dimethyldodecylamine N-oxide is not an efficient substrate for the enzyme
392775
Shewanella massilia
N,N-dimethyldodecylamine + H2O + oxidized electron donor
-
392775
Shewanella massilia
?
trimethylamine N-oxide + electron donor
-
392775
Shewanella massilia
trimethylamine + oxidized electron donor + H2O
-
392775
Shewanella massilia
?
trimethylamine-N-oxide + electron donor
-
392775
Shewanella massilia
trimethylamine + oxidized electron donor + H2O
-
392775
Shewanella massilia
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 90000, SDS-PAGE
Shewanella massilia
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4
-
dibutylsulfoxide
value below
Shewanella massilia
4
-
Dimethylsulfoxide
value below
Shewanella massilia
4
-
diphenylsulfoxide
value below
Shewanella massilia
4
-
DL-methioninesulfoxide
value below
Shewanella massilia
78
-
alpha-picoline N-oxide
-
Shewanella massilia
109
-
4-methylmorpholine N-oxide
-
Shewanella massilia
120
-
Trimethylamine N-oxide
-
Shewanella massilia
151
-
N,N-dimethyldodecylamine N-oxide
-
Shewanella massilia
Other publictions for EC 1.7.2.3
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)
743776
Lemaire
Efficient respiration on TMAO ...
Shewanella oneidensis
Res. Microbiol.
167
630-637
2016
-
-
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-
-
-
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4
-
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1
1
-
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-
687081
Zhang
Structure of the molybdenum si ...
Escherichia coli
Inorg. Chem.
47
1074-1078
2008
-
-
1
-
-
-
-
-
-
2
-
1
-
3
-
-
-
1
-
-
-
-
2
1
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-
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1
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1
1
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2
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1
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2
1
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687424
Dunn
Genetic analysis of trimethyla ...
Aliivibrio fischeri, Aliivibrio fischeri ES114, Euprymna scolopes
J. Bacteriol.
190
5814-5823
2008
-
-
2
-
3
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1
-
15
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1
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1
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2
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3
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1
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1
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1
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-
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-
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-
700261
Ansaldi
Aerobic TMAO respiration in Es ...
Escherichia coli
Mol. Microbiol.
66
484-494
2007
1
-
1
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
-
-
-
2
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-
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-
-
1
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1
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1
1
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-
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-
1
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-
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-
2
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-
-
-
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-
671735
Genest
Signal peptide protection by s ...
Escherichia coli
Biochem. Biophys. Res. Commun.
339
991-995
2006
1
-
1
-
-
-
-
-
-
1
1
-
-
1
-
-
1
-
-
-
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-
-
1
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-
-
-
-
-
-
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-
-
1
-
1
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-
-
-
-
-
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-
-
1
1
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
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-
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-
654560
Hatzixanthis
Chaperones involved in assembl ...
Escherichia coli, Shewanella massilia
Biochem. Soc. Trans.
33
124-126
2005
-
-
2
-
-
-
-
-
2
1
-
1
-
3
-
-
1
-
-
-
-
-
1
3
-
-
-
-
-
-
-
1
-
-
-
-
-
2
1
-
-
-
-
-
-
-
2
1
-
1
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-
-
1
-
-
-
-
1
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
656279
Genest
TorD, an essential chaperone f ...
Escherichia coli
J. Biol. Chem.
280
15644-15648
2005
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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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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-
-
-
-
-
-
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-
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676796
Hatzixanthis
Signal peptide-chaperone inter ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
102
8460-8465
2005
-
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-
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1
1
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-
3
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1
1
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-
655851
Bordi
Effects of ISSo2 insertions in ...
Shewanella oneidensis
J. Bacteriol.
185
2042-2045
2003
-
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1
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-
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-
2
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2
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3
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1
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1
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1
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2
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3
-
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656147
Ilbert
Involvement of a mate chaperon ...
Escherichia coli
J. Biol. Chem.
278
28787-28792
2003
-
-
1
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-
-
-
-
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1
1
-
4
-
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1
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1
1
1
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1
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1
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1
1
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1
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1
1
1
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1
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-
-
-
-
-
-
-
-
392780
Gon
Reconstitution of the trimethy ...
Shewanella oneidensis
J. Bacteriol.
184
1262-1269
2002
-
-
1
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-
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6
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1
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657290
Tranier
Characterization and multiple ...
Shewanella massilia
Protein Sci.
11
2148-2157
2002
-
-
1
1
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1
-
8
1
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1
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1
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1
3
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1
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1
1
1
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1
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8
1
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1
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1
3
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437732
Gon
Electron transfer and binding ...
Escherichia coli
J. Biol. Chem.
276
11545-11551
2001
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1
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3
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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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437733
Gon
An unsuspected autoregulatory ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
98
11615-11620
2001
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-
1
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-
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1
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2
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1
-
-
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-
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-
1
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-
1
1
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-
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1
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1
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437734
Gon
The torYZ (yecK bisZ) operon e ...
Escherichia coli
J. Bacteriol.
182
5779-5786
2000
-
-
1
-
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-
4
1
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2
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-
1
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-
-
4
-
-
-
-
-
-
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-
1
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-
1
1
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-
-
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-
-
4
1
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-
1
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4
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392776
Buc
Enzymatic and physiological pr ...
Escherichia coli
Mol. Microbiol.
32
159-168
1999
-
-
-
-
-
1
-
16
-
1
-
-
-
2
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-
-
-
-
-
1
-
10
-
2
-
1
16
2
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
16
-
1
-
-
-
-
-
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1
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10
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2
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1
16
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392777
Ansaldi
TorC apocytochrome negatively ...
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392778
Mikhaleva
Requirement for phospholipids ...
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1999
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392771
Czjzek
Crystal structure of oxidized ...
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392774
Pommier
TorD, a cytoplasmic chaperone ...
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5
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392775
Dos Santos
Molecular analysis of the trim ...
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437735
Knäblein
Isolation, cloning, sequence a ...
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Iobbi-Nivol
High substrate specificity and ...
Escherichia coli
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437737
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TMAO anaerobic respiration in ...
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Sajitz
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Isolation and properties of tr ...
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Arata
Purification and properties of ...
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2
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392761
Yamamoto
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Anaerobic induction of trimeth ...
Escherichia coli
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392762
Silvestro
The inducible trimethylamine N ...
Escherichia coli
Biochim. Biophys. Acta
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208-216
1989
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392763
McEwan
-
Identification of cytochromes ...
Rhodobacter capsulatus
Biochim. Biophys. Acta
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308-314
1989
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392758
Clarke
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Purification and properties of ...
Shewanella sp.
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1988
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392764
Arata
Trimethylamine N-oxide respira ...
Erythrobacter sp., Erythrobacter sp. Och 114
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1988
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392765
Silvestro
The inducible trimethylamine-N ...
Escherichia coli
Biochim. Biophys. Acta
954
1-13
1988
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6
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2
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6
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2
1
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2
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392766
McEwan
-
The periplasmic nitrate reduct ...
Rhodobacter capsulatus
Biochem. Soc. Trans.
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182-183
1988
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1
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3
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392757
Yamamoto
Further characterization of tr ...
Escherichia coli
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1773-1779
1986
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5
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2
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2
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2
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2
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4
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4
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3
2
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5
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2
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2
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392756
Violet
-
Trimethylamine N-oxide (TMAO) ...
Escherichia coli
FEMS Microbiol. Lett.
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85-91
1985
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2
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392767
Styrvold
Dimethylsulfoxide and trimethy ...
Proteus vulgaris
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74-78
1984
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3
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392755
Kwan
Purification and properties of ...
Salmonella enterica subsp. enterica serovar Typhimurium
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1455-1458
1983
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1
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1
2
6
1
1
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3
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1
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2
1
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1
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9
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2
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2
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1
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1
2
6
1
1
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3
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1
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392768
Easter
-
The induction and location of ...
Alteromonas sp.
J. Gen. Microbiol.
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3689-3696
1983
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6
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1
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1
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6
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4
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392769
Bragg
Cytochromes of the trimethylam ...
Escherichia coli
Biochim. Biophys. Acta
725
168-177
1983
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4
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1
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2
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4
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392770
Kwan
Roles for menaquinone and the ...
Salmonella enterica subsp. enterica serovar Typhimurium
J. Bacteriol.
155
1147-1155
1983
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12
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3
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12
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3
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392759
Cox
-
Trimethylamine N-oxide (TMAO) ...
Escherichia coli
FEMS Microbiol. Lett.
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249-252
1981
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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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