BRENDA - Enzyme Database show
show all sequences of 1.20.4.4

Arsenate reductase of Staphylococcus aureus plasmid pI258

Ji, G.; Garber, E.A.E.; Armes, L.G.; Chen, C.M.; Fuchs, J.A.; Silver, S.; Biochemistry 33, 7294-7299 (1994)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
overproduced in Escherichia coli
Staphylococcus aureus
Inhibitors
Inhibitors
Commentary
Organism
Structure
antimonite
SbO2-, pH 7.5, 37°C
Staphylococcus aureus
arsenite
pH 7.5, 37°C
Staphylococcus aureus
additional information
arsenite, tellurite, and antimonite [Sb(III)] are inhibitors for NADPH oxidation; the substrate, arsenate, is not inhibitory at concentrations up to 40 mM
Staphylococcus aureus
tellurite
pH 7.5, 37°C
Staphylococcus aureus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
arsenate
pH 7.5, 37°C, at low substrate concentrations the Km-value for arsenate is 0.0008 mM. Above 1 mM arsenate, a second increase in rate with increasing substrate is observed, with an apparent Km of 2 mM arsenate
Staphylococcus aureus
additional information
-
additional information
NADPH oxidation shows Michaelis-Menten kinetics with a Km of 1 microM AsO43- and an apparent Vmax of 200 nmol/min per mg of protein. At high substrate concentration (above 1 mM AsO43-), a secondary rise in the reaction rate is observed, with a Km of 2 mM and an apparent Vmax of 450 nmol/min per mg of protein
Staphylococcus aureus
0.0008
-
arsenate
high affinity
Staphylococcus aureus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
14436
-
x * 14436, protein with a loss of the first three amino acid residues from part of the arsenate reductase may have occurred intracellularly or extracellularly during the purification process, mass spectral analysis
Staphylococcus aureus
14440
-
calculated from amino acid sequence
Staphylococcus aureus
14500
-
electrospray mass spectrometry shows two molecular masses of 14810.5 and 14436.0 Da, suggesting that 70% of the purified protein lacks the N-terminal three amino acids
Staphylococcus aureus
14810
-
x * 14810, full length enzyme, mass spectral analysis
Staphylococcus aureus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
arsenate + thioredoxin
Staphylococcus aureus
-
arsenite + thioredoxin disulfide + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Staphylococcus aureus
P0A006
-
-
Purification (Commentary)
Commentary
Organism
; gel filtration, SDS-PAGE
Staphylococcus aureus
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.2
-
pH 7.5, 37°C
Staphylococcus aureus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
arsenate + thioredoxin
-
639368
Staphylococcus aureus
arsenite + thioredoxin disulfide + H2O
-
-
-
?
arsenate + thioredoxin
glutaredoxin and reduced glutathione does not stimulate arsenate reduction
639368
Staphylococcus aureus
arsenite + thioredoxin disulfide + H2O
-
-
-
?
additional information
selenate is a poor substrate
639368
Staphylococcus aureus
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 14436, protein with a loss of the first three amino acid residues from part of the arsenate reductase may have occurred intracellularly or extracellularly during the purification process, mass spectral analysis; x * 14810, full length enzyme, mass spectral analysis
Staphylococcus aureus
monomer
-
Staphylococcus aureus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Staphylococcus aureus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Staphylococcus aureus
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
purified enzyme reduces radioactive arsenate to arsenite when coupled to thioredoxin, thioredoxin reductase, and NADPH. All three protein components, arsenate reductase, thioredoxin, and thioredoxin reductase, are required for arsenate reduction. Glutaredoxin and reduced glutathione do not stimulate arsenate reduction
Staphylococcus aureus
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0005
-
tellurite
pH 7.5, 37°C
Staphylococcus aureus
0.01
-
antimonite
pH 7.5, 37°C
Staphylococcus aureus
0.5
-
arsenite
pH 7.5, 37°C
Staphylococcus aureus
Cloned(Commentary) (protein specific)
Commentary
Organism
overproduced in Escherichia coli
Staphylococcus aureus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
purified enzyme reduces radioactive arsenate to arsenite when coupled to thioredoxin, thioredoxin reductase, and NADPH. All three protein components, arsenate reductase, thioredoxin, and thioredoxin reductase, are required for arsenate reduction. Glutaredoxin and reduced glutathione do not stimulate arsenate reduction
Staphylococcus aureus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
antimonite
SbO2-, pH 7.5, 37°C
Staphylococcus aureus
arsenite
pH 7.5, 37°C
Staphylococcus aureus
additional information
arsenite, tellurite, and antimonite [Sb(III)] are inhibitors for NADPH oxidation; the substrate, arsenate, is not inhibitory at concentrations up to 40 mM
Staphylococcus aureus
tellurite
pH 7.5, 37°C
Staphylococcus aureus
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0005
-
tellurite
pH 7.5, 37°C
Staphylococcus aureus
0.01
-
antimonite
pH 7.5, 37°C
Staphylococcus aureus
0.5
-
arsenite
pH 7.5, 37°C
Staphylococcus aureus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
arsenate
pH 7.5, 37°C, at low substrate concentrations the Km-value for arsenate is 0.0008 mM. Above 1 mM arsenate, a second increase in rate with increasing substrate is observed, with an apparent Km of 2 mM arsenate
Staphylococcus aureus
additional information
-
additional information
NADPH oxidation shows Michaelis-Menten kinetics with a Km of 1 microM AsO43- and an apparent Vmax of 200 nmol/min per mg of protein. At high substrate concentration (above 1 mM AsO43-), a secondary rise in the reaction rate is observed, with a Km of 2 mM and an apparent Vmax of 450 nmol/min per mg of protein
Staphylococcus aureus
0.0008
-
arsenate
high affinity
Staphylococcus aureus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
14436
-
x * 14436, protein with a loss of the first three amino acid residues from part of the arsenate reductase may have occurred intracellularly or extracellularly during the purification process, mass spectral analysis
Staphylococcus aureus
14440
-
calculated from amino acid sequence
Staphylococcus aureus
14500
-
electrospray mass spectrometry shows two molecular masses of 14810.5 and 14436.0 Da, suggesting that 70% of the purified protein lacks the N-terminal three amino acids
Staphylococcus aureus
14810
-
x * 14810, full length enzyme, mass spectral analysis
Staphylococcus aureus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
arsenate + thioredoxin
Staphylococcus aureus
-
arsenite + thioredoxin disulfide + H2O
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
; gel filtration, SDS-PAGE
Staphylococcus aureus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.2
-
pH 7.5, 37°C
Staphylococcus aureus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
arsenate + thioredoxin
-
639368
Staphylococcus aureus
arsenite + thioredoxin disulfide + H2O
-
-
-
?
arsenate + thioredoxin
glutaredoxin and reduced glutathione does not stimulate arsenate reduction
639368
Staphylococcus aureus
arsenite + thioredoxin disulfide + H2O
-
-
-
?
additional information
selenate is a poor substrate
639368
Staphylococcus aureus
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 14436, protein with a loss of the first three amino acid residues from part of the arsenate reductase may have occurred intracellularly or extracellularly during the purification process, mass spectral analysis; x * 14810, full length enzyme, mass spectral analysis
Staphylococcus aureus
monomer
-
Staphylococcus aureus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Staphylococcus aureus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Staphylococcus aureus
Other publictions for EC 1.20.4.4
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)
745640
Politi
Arsenate reductase from Therm ...
Thermus thermophilus
J. R. Soc. Interface
13
20160629
2016
-
-
-
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-
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-
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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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-
-
-
-
732190
Nunes
ArsC3 from Desulfovibrio alask ...
Desulfovibrio alaskensis, Desulfovibrio alaskensis G20
J. Biol. Inorg. Chem.
19
1277-1285
2014
-
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1
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3
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2
4
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-
14
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-
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2
1
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3
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1
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1
1
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3
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2
4
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-
2
1
-
-
-
3
-
-
-
-
-
1
1
-
3
3
727086
Del Giudice
A novel arsenate reductase fro ...
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Biochim. Biophys. Acta
1834
2071-2079
2013
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1
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1
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1
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2
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8
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1
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1
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1
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1
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2
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1
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4
1
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1
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1
1
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1
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-
726005
Villadangos
Corynebacterium glutamicum sur ...
Corynebacterium glutamicum, Corynebacterium glutamicum DSM 20300
Mol. Microbiol.
82
998-1014
2011
-
-
1
1
1
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-
2
-
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2
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2
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2
2
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2
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2
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1
2
1
1
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2
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2
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-
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-
2
2
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2
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1
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1
2
2
714404
Yu
(1)H, (13)C and (15)N resonanc ...
Microbacterium sp.
Biomol. NMR Assign.
5
85-87
2010
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-
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2
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1
2
4
1
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-
715567
Wu
Novel channel enzyme fusion pr ...
Salinispora tropica
J. Biol. Chem.
285
40081-40087
2010
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1
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1
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1
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1
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1
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1
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1
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1
1
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1
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1
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1
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1
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2
2
-
1
1
674785
Li
Conformational fluctuations co ...
Bacillus subtilis
J. Biol. Chem.
282
11078-11083
2007
-
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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
1
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1
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705113
Roos
Interplay between ion binding ...
Bacillus subtilis, Staphylococcus aureus
J. Mol. Biol.
360
826-838
2006
2
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2
2
8
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-
12
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5
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2
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2
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11
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2
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2
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2
8
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12
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2
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2
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11
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12
12
701458
Messens
The structure of a triple muta ...
Staphylococcus aureus
Acta Crystallogr. Sect. D
60
1180-1184
2004
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1
1
1
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705110
Messens
How thioredoxin can reduce a b ...
Staphylococcus aureus
J. Mol. Biol.
339
527-537
2004
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1
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3
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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
1
639369
Messens
Development of a downstream pr ...
Staphylococcus aureus
J. Chromatogr. B
737
167-178
2000
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1
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4
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2
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1
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1
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1
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1
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639370
Messens
The essential catalytic redox ...
Staphylococcus aureus
Biochemistry
38
16857-16865
1999
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1
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9
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2
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2
2
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1
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1
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4
1
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1
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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4
1
1
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4
1
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1
1
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4
4
639368
Ji
Arsenate reductase of Staphylo ...
Staphylococcus aureus
Biochemistry
33
7294-7299
1994
-
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1
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4
3
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4
1
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1
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1
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1
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3
2
1
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1
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1
3
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1
1
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4
3
3
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4
1
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1
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1
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3
2
1
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1
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706565
Ji
Reduction of arsenate to arsen ...
Staphylococcus aureus subsp. aureus RN4220
Proc. Natl. Acad. Sci. USA
89
9474-9478
1992
3
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1
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2
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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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