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arsenate + thioredoxin
arsenite + thioredoxin disulfide + H2O
additional information
?
-
arsenate + thioredoxin
arsenite + thioredoxin disulfide + H2O
-
-
-
?
arsenate + thioredoxin
arsenite + thioredoxin disulfide + H2O
-
-
-
?
arsenate + thioredoxin
arsenite + thioredoxin disulfide + H2O
-
-
-
?
arsenate + thioredoxin
arsenite + thioredoxin disulfide + H2O
Oleidesulfovibrio alaskensis
-
-
-
-
?
arsenate + thioredoxin
arsenite + thioredoxin disulfide + H2O
Oleidesulfovibrio alaskensis G20
-
-
-
-
?
arsenate + thioredoxin
arsenite + thioredoxin disulfide + H2O
-
-
-
-
?
arsenate + thioredoxin
arsenite + thioredoxin disulfide + H2O
-
-
-
?
arsenate + thioredoxin
arsenite + thioredoxin disulfide + H2O
-
-
-
-
?
arsenate + thioredoxin
arsenite + thioredoxin disulfide + H2O
-
-
-
?
arsenate + thioredoxin
arsenite + thioredoxin disulfide + H2O
the enzyme encoded by Staphylococcus aureus arsenic-resistance plasmid pI258 reduces intracellular arsenate to the more toxic arsenite, which is subsequently extruded from the cell
-
-
?
arsenate + thioredoxin
arsenite + thioredoxin disulfide + H2O
glutaredoxin and reduced glutathione does not stimulate arsenate reduction
-
-
?
arsenate + thioredoxin
arsenite + thioredoxin disulfide + H2O
the enzyme uses an intramolecular thiol pair (Cys82, Cys89) for the reduction of arsenate
-
-
?
arsenate + thioredoxin
arsenite + thioredoxin disulfide + H2O
-
-
-
?
arsenate + thioredoxin
arsenite + thioredoxin disulfide + H2O
-
-
-
-
?
arsenate + thioredoxin
arsenite + thioredoxin disulfide + H2O
-
-
-
?
arsenate + thioredoxin
arsenite + thioredoxin disulfide + H2O
-
-
-
?
additional information
?
-
assays are performed with different arsenate concentrations and arsenate reductase concentrations in the presence of 0.42 microM Escherichia coli thioredoxin, 0.14 microM Escherichia coli thioredoxin reductase and 125 microM NADPH
-
-
?
additional information
?
-
selenate is a poor substrate
-
-
?
additional information
?
-
enzyme additionally exhibits weak phosphatase activity
-
-
?
additional information
?
-
-
enzyme additionally exhibits weak phosphatase activity
-
-
?
additional information
?
-
enzyme additionally exhibits weak phosphatase activity
-
-
?
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additional information
arsenate
0.000066
arsenate
wild-type
0.000066
arsenate
pH 7.5, 37°C, wild-type enzyme
0.000134
arsenate
C15A mutant
0.000134
arsenate
pH 7.5, 37°C, mutant enzyme C15A
0.0008
arsenate
high affinity
0.006
arsenate
Oleidesulfovibrio alaskensis
-
pH 7.6, 37°C, presence of 150 mM KCl
0.007
arsenate
Oleidesulfovibrio alaskensis
-
pH 7.6, 37°C, presence of 50 mM K2SO4
0.008
arsenate
Oleidesulfovibrio alaskensis
-
pH 7.6, 37°C, presence of 150 mM NaCl
0.009
arsenate
wild-type Staphylococcus aureus, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
0.022
arsenate
wild-type Staphylococcus aureus, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
0.032
arsenate
wild-type, pH 8.0, 37°C
0.047
arsenate
wild-type Bacillus subtilis, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
0.054
arsenate
wild-type Bacillus subtilis, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
0.058
arsenate
wild-type Bacillus subtilis, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
0.061
arsenate
wild-type Staphylococcus aureus, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
0.064
arsenate
wild-type Bacillus subtilis, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
0.08
arsenate
H62Q mutant Staphylococcus aureus, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
0.081
arsenate
wild-type Staphylococcus aureus, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
0.087
arsenate
H62Q mutant Staphylococcus aureus, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
0.11
arsenate
N-terminally truncated mutant, pH 8.0, 37°C
0.123
arsenate
H62Q mutant Staphylococcus aureus, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
0.131
arsenate
H62Q mutant Staphylococcus aureus, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
0.635
arsenate
pH 7.0, 60°C
75
arsenate
-
pH 7.5, temperature not specified in the publication
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
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
-
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0.061
arsenate
C15A ArsC mutant, at 2 microM AsO43-
0.061
arsenate
pH 7.5, 37°C, mutant enzyme C15A, at 0.002 mM arsenate
0.075
arsenate
wild-type ArsC, at 2 microM AsO43-
0.075
arsenate
pH 7.5, 37°C, wild-type enzyme, at 0.002 mM arsenate
0.08
arsenate
C15A ArsC mutant, at 10 mM AsO43-
0.08
arsenate
pH 7.5, 37°C, mutant enzyme C15A, at 10 mM arsenate
0.09
arsenate
wild-type, pH 8.0, 37°C
0.165
arsenate
wild-type ArsC, at 10 mM AsO43-
0.165
arsenate
pH 7.5, 37°C, wild-type enzyme, at 10 mM arsenate
0.5
arsenate
N-terminally truncated mutant, pH 8.0, 37°C
0.58
arsenate
wild-type Staphylococcus aureus, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
0.7
arsenate
H62Q mutant Staphylococcus aureus, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
0.75
arsenate
pH 7.0, 60°C
0.75
arsenate
H62Q mutant Staphylococcus aureus, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
0.9
arsenate
wild-type Staphylococcus aureus, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
1.3
arsenate
wild-type Bacillus subtilis, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
1.6
arsenate
wild-type Bacillus subtilis, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
1.6
arsenate
wild-type Bacillus subtilis, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
1.98
arsenate
H62Q mutant Staphylococcus aureus, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
2
arsenate
wild-type Bacillus subtilis, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
2.1
arsenate
Oleidesulfovibrio alaskensis
-
pH 7.6, 37°C, presence of 150 mM NaCl
2.9
arsenate
wild-type Staphylococcus aureus, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
2.9
arsenate
Oleidesulfovibrio alaskensis
-
pH 7.6, 37°C, presence of 50 mM K2SO4
3.03
arsenate
H62Q mutant Staphylococcus aureus, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
3.2
arsenate
Oleidesulfovibrio alaskensis
-
pH 7.6, 37°C, presence of 150 mM KCl
3.65
arsenate
wild-type Staphylococcus aureus, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
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0.045
arsenate
N-terminally truncated mutant, pH 8.0, 37°C
0.21
arsenate
-
pH 7.5, temperature not specified in the publication
2.9
arsenate
wild-type, pH 8.0, 37°C
6.1
arsenate
H62Q mutant Staphylococcus aureus, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
8.1
arsenate
H62Q mutant Staphylococcus aureus, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
22.4
arsenate
wild-type Bacillus subtilis, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
23.1
arsenate
H62Q mutant Staphylococcus aureus, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
24.8
arsenate
H62Q mutant Staphylococcus aureus, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
26.4
arsenate
wild-type Staphylococcus aureus, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
29.6
arsenate
wild-type Bacillus subtilis, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
31.3
arsenate
wild-type Bacillus subtilis, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
34
arsenate
wild-type Bacillus subtilis, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
45.1
arsenate
wild-type Staphylococcus aureus, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
47.5
arsenate
wild-type Staphylococcus aureus, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
100
arsenate
wild-type Staphylococcus aureus, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
256
arsenate
Oleidesulfovibrio alaskensis
-
pH 7.6, 37°C, presence of 150 mM NaCl
409
arsenate
Oleidesulfovibrio alaskensis
-
pH 7.6, 37°C, presence of 50 mM K2SO4
441
arsenate
pH 7.5, 37°C, mutant enzyme C15A, at 0.002 mM arsenate
455
arsenate
C15A mutant, 2.6 times lower
531
arsenate
Oleidesulfovibrio alaskensis
-
pH 7.6, 37°C, presence of 150 mM KCl
1170
arsenate
pH 7.5, 37°C, wild-type enzyme, at 0.002 mM arsenate
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malfunction
ArsC3 together with ArsC1 is able to rescue the arsenate sensitivity phenotype of Escherichia coli mutant AW3110
malfunction
ArsC3 together with ArsC1 is able to rescue the arsenate sensitivity phenotype of Escherichia coli mutant AW3110. ArsC1 is the major contributor of arsenate resistance in Escherichia coli
malfunction
-
heterologous expression of Strop634 or its separate arsenate reductase domain complements a yeast strain lacking arsenate reductase acr2
malfunction
-
Salinispora tropica Strop634 deletion strains are highly sensitive to arsenate exposure
physiological function
ArsC1 functions as an arsenate reductase required for As(V) detoxification
physiological function
ArsC1 is part of a gene cluster consisting of pair of genes (arsTX) encoding a thioredoxin system that are cotranscribed with an unusual arsRC2 fusion gene, ACR3, and arsC1 in an operon divergent from arsC3. The whole arsenic resistance system gene cluster is required to fully complement an Escherichia coli ars mutant AW3110 (strain lacking the arsenic resistance system operon)
physiological function
ArsC3 functions as arsenate reductase required for As(V) detoxification
physiological function
ArsC3 is part of a gene cluster consisting of pair of genes (arsTX) encoding a thioredoxin system that are cotranscribed with an unusual arsRC2 fusion gene, ACR3, and arsC1 in an operon divergent from arsC3. The whole arsenic resistance system gene cluster is required to fully complement an Escherichia coli ars mutant AW3110 (strain lacking the arsenic resistance system operon)
physiological function
-
as a dual functional protein (arsenite channel and arsenate reductase) Strop634 rescues a yeast strain that is highly sensitive to arsenate due to deletion of the ACR2 reductase and all transport proteins for arsenite, ACR3, Fps1, and the vacuolar ABC transporter Ycf1 for arsenite-thiol conjugates
physiological function
-
confers arsenate resistance in Salinispora tropica
physiological function
Oleidesulfovibrio alaskensis
-
isoform ArsC3 is functional and able to confer arsenate resistance to Escherichia coli
physiological function
the enzyme encoded by Staphylococcus aureus arsenic-resistance plasmid pI258 reduces intracellular arsenate to the more toxic arsenite, which is subsequently extruded from the cell
physiological function
Oleidesulfovibrio alaskensis G20
-
isoform ArsC3 is functional and able to confer arsenate resistance to Escherichia coli
-
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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
14440
calculated from amino acid sequence
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
14800
reduced C82S mutant
14820
reduced C89L mutant
15030
calculated, SDS-PAGE
16000
Oleidesulfovibrio alaskensis
-
1 * 16010, calculated, 1 * 16000, SDS-PAGE, 1 * 16008, ESI-microTOF
16008
Oleidesulfovibrio alaskensis
-
1 * 16010, calculated, 1 * 16000, SDS-PAGE, 1 * 16008, ESI-microTOF
16010
Oleidesulfovibrio alaskensis
-
1 * 16010, calculated, 1 * 16000, SDS-PAGE, 1 * 16008, ESI-microTOF
16957
1 * 16957, calculated, 1 * 17000, SDS-PAGE
20000
Oleidesulfovibrio alaskensis
-
gel filtration
25360
2 * 25360, SDS-PAGE
14400
-
14810
calculated, reduced form
14810
x * 14810, full length enzyme, mass spectral analysis
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?
x * 14400, SDS-PAGE
?
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
dimer
2 * 25360, SDS-PAGE
dimer
-
2 * 25360, SDS-PAGE
-
monomer
Oleidesulfovibrio alaskensis
-
1 * 16010, calculated, 1 * 16000, SDS-PAGE, 1 * 16008, ESI-microTOF
monomer
Oleidesulfovibrio alaskensis G20
-
1 * 16010, calculated, 1 * 16000, SDS-PAGE, 1 * 16008, ESI-microTOF
-
monomer
1 * 16957, calculated, 1 * 17000, SDS-PAGE
monomer
-
1 * 16957, calculated, 1 * 17000, SDS-PAGE
-
additional information
isoform ArsC1' is unique in bearing an N-terminal three-helical bundle that interacts with the active site of the other chain in the dimeric interface
additional information
-
isoform ArsC1' is unique in bearing an N-terminal three-helical bundle that interacts with the active site of the other chain in the dimeric interface
-
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C10S/C15A/C82S
mutant in complex with the thioredoxin C32S mutant. Solve the structure of the Trx-ArsC complex by NMR spectroscopy
K33D
site directed mutagenesis
K33N
site directed mutagenesis
C10S/C15A/C89L
mutant, determination of the redox potential of the Cys82-Cys89 redox couple
C10S/C15S
double mutation, no enzymatic activity
C10SC15A
inactive mutant enzyme
H62Q
change of the P-loop geometry
H62Q/N33K
site directed mutagenesis
H62Q/N33K/E30D/G31E
site directed mutagenesis
C10A
site-directed mutagenesis
C10A
inactive mutant enzyme
C10A
site-directed mutagenesis, mutation of Cys 10, 82, and 89 leads to redox-inactive enzymes
C10S/C15A
change of the P-loop geometry
C10S/C15A
double mutation, no enzymatic activity
C10S/C15A/C82S
mutant, determination of the redox potential of the Cys82-Cys89 redox couple, thioredoxin is unable to reduce the Cys10-Cys15 disulfide in oxidized ArsC C82S
C10S/C15A/C82S
site-directed mutagenesis, triple mutant, structure very similar to that of the reduced form of wild-type ArsC
C15A
site-directed mutagenesis
C15A
site-directed mutagenesis, only ArsC wild type and ArsC C15A show enzymatic activity
C15A
as compared to wild-type enzyme the affinity is reduced ba a factor of 2
C82A
site-directed mutagenesis
C82A
site-directed mutagenesis, mutation of Cys 10, 82, and 89 leads to redox-inactive enzymes
C82S
inactive mutant enzyme
C82S
site-directed mutagenesis, mutation of Cys 10, 82, and 89 leads to redox-inactive enzymes
C89A
site-directed mutagenesis
C89A
inactive mutant enzyme
C89A
site-directed mutagenesis, mutation of Cys 10, 82, and 89 leads to redox-inactive enzymes
C7S
complete loss of activity
C7S
-
complete loss of activity
-
additional information
commonly occurring mutation of a histidine (H62), located about 6 A from the potassium-binding site in Sa_ArsC, to a glutamine uncouples the kinetic dependency on potassium. Mutations within the Trx-coupled family of arsenate reductases lead to subtly different ion-dependent kinetic features
additional information
-
commonly occurring mutation of a histidine (H62), located about 6 A from the potassium-binding site in Sa_ArsC, to a glutamine uncouples the kinetic dependency on potassium. Mutations within the Trx-coupled family of arsenate reductases lead to subtly different ion-dependent kinetic features
additional information
in mutant lacking N-terminal 78 amino acids, the kinetic parameters are greatly reduced
additional information
-
in mutant lacking N-terminal 78 amino acids, the kinetic parameters are greatly reduced
-
additional information
ArsC triple mutants and the Trx C32S mutant formate a ArsC-TrxC32S complex
additional information
-
ArsC triple mutants and the Trx C32S mutant formate a ArsC-TrxC32S complex
additional information
commonly occurring mutation of a histidine (H62), located about 6 A from the potassium-binding site in Sa_ArsC, to a glutamine uncouples the kinetic dependency on potassium. Mutations within the Trx-coupled family of arsenate reductases lead to subtly different ion-dependent kinetic features
additional information
-
commonly occurring mutation of a histidine (H62), located about 6 A from the potassium-binding site in Sa_ArsC, to a glutamine uncouples the kinetic dependency on potassium. Mutations within the Trx-coupled family of arsenate reductases lead to subtly different ion-dependent kinetic features
additional information
essential cysteinyl residues and redox couple in arsenate reductase are identified by a combination of site-specific mutagenesis and endoprotease-digest mass spectroscopy analysis
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C10S/C15A/C89L mutant and C10S/C15A/C82S mutant expressed in Escherichia coli
expressed in Escherichia coli
expressed in Escherichia coli and yeast
-
expression in Escherichia coli
expression in Escherichia coli. Wild-type enzyme and the Cys mutants (C15A, C10A, C82A, C82S, C89A, C10SC15S, C10SC15A) are expressed in Escherichia coli. Wild-type enzyme, mutant enzyme C15A, mutant enzyme C10A, mutant enzyme C82S, mutant enzyme C89A, and mutant enzyme C10SC15A are expressed soluble and with high yields. Mutant enzyme C82A is found in inclusion bodies, and the double mutant C10S/C15S is not expressed
mutant expressed in Escherichia coli
mutant is expressed in Escherichia coli
overproduced in Escherichia coli
overproduced in Escherichia coli K38(pGP1-2)
expressed in Escherichia coli
expressed in Escherichia coli
-
expressed in Escherichia coli
expression in Escherichia coli
Oleidesulfovibrio alaskensis
-
expression in Escherichia coli
expression in Escherichia coli
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Ji, G.; Garber, E.A.E.; Armes, L.G.; Chen, C.M.; Fuchs, J.A.; Silver, S.
Arsenate reductase of Staphylococcus aureus plasmid pI258
Biochemistry
33
7294-7299
1994
Staphylococcus aureus (P0A006)
brenda
Messens, J.; Hayburn, G.; Brosens, E.; Laus, G.; Wyns, L.
Development of a downstream process for the isolation of Staphylococcus aureus arsenate reductase overproduced in Escherichia coli
J. Chromatogr. B
737
167-178
2000
Staphylococcus aureus (P0A006)
brenda
Messens, J.; Hayburn, G.; Desmyter, A.; Laus, G.; Wyns, L.
The essential catalytic redox couple in arsenate reductase from Sataphylococcus aureus
Biochemistry
38
16857-16865
1999
Staphylococcus aureus (P0A006)
brenda
Li, Y.; Hu, Y.; Zhang, X.; Xu, H.; Lescop, E.; Xia, B.; Jin, C.
Conformational fluctuations coupled to the thiol-disulfide transfer between thioredoxin and arsenate reductase in Bacillus subtilis
J. Biol. Chem.
282
11078-11083
2007
Bacillus subtilis (P45947), Bacillus subtilis
brenda
Messens, J.; Van Molle, I.; Vanhaesebrouck, P.; Van Belle, K.; Wahni, K.; Martins, J.C.; Wyns, L.; Loris, R.
The structure of a triple mutant of pI258 arsenate reductase from Staphylococcus aureus and its 5-thio-2-nitrobenzoic acid adduct
Acta Crystallogr. Sect. D
60
1180-1184
2004
Staphylococcus aureus (P0A006), Staphylococcus aureus
brenda
Messens, J.; Van Molle, I.; Vanhaesebrouck, P.; Limbourg, M.; Van Belle, K.; Wahni, K.; Martins, J.C.; Loris, R.; Wyns, L.
How thioredoxin can reduce a buried disulphide bond
J. Mol. Biol.
339
527-537
2004
Staphylococcus aureus (P0A006), Staphylococcus aureus
brenda
Roos, G.; Buts, L.; Van Belle, K.; Brosens, E.; Geerlings, P.; Loris, R.; Wyns, L.; Messens, J.
Interplay between ion binding and catalysis in the thioredoxin-coupled arsenate reductase family
J. Mol. Biol.
360
826-838
2006
Staphylococcus aureus (P0A006), Staphylococcus aureus, Bacillus subtilis (P45947), Bacillus subtilis
brenda
Ji, G.; Silver, S.
Reduction of arsenate to arsenite by the ArsC protein of the arsenic resistance operon of Staphylococcus aureus plasmid pI258
Proc. Natl. Acad. Sci. USA
89
9474-9478
1992
Staphylococcus aureus subsp. aureus RN4220 (P0A006)
brenda
Yu, C.; Xia, B.; Jin, C.
(1)H, (13)C and (15)N resonance assignments of the arsenate reductase from Synechocystis sp. strain PCC 6803
Biomol. NMR Assign.
5
85-87
2010
Microbacterium sp. (B7FAZ6), Microbacterium sp. (B7FB01)
brenda
Wu, B.; Song, J.; Beitz, E.
Novel channel enzyme fusion proteins confer arsenate resistance
J. Biol. Chem.
285
40081-40087
2010
Salinispora tropica
brenda
Villadangos, A.F.; Van Belle, K.; Wahni, K.; Dufe, V.T.; Freitas, S.; Nur, H.; De Galan, S.; Gil, J.A.; Collet, J.F.; Mateos, L.M.; Messens, J.
Corynebacterium glutamicum survives arsenic stress with arsenate reductases coupled to two distinct redox mechanisms
Mol. Microbiol.
82
998-1014
2011
Corynebacterium glutamicum (P0DKS5), Corynebacterium glutamicum DSM 20300 (P0DKS5)
brenda
Del Giudice, I.; Limauro, D.; Pedone, E.; Bartolucci, S.; Fiorentino, G.
A novel arsenate reductase from the bacterium Thermus thermophilus HB27: its role in arsenic detoxification
Biochim. Biophys. Acta
1834
2071-2079
2013
Thermus thermophilus (Q72HI5), Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (Q72HI5)
brenda
Nunes, C.; Bras, J.; Najmudin, S.; Moura, J.; Moura, I.; Carepo, M.
ArsC3 from Desulfovibrio alaskensis G20, a cation and sulfate-independent highly efficient arsenate reductase
J. Biol. Inorg. Chem.
19
1277-1285
2014
Oleidesulfovibrio alaskensis, Oleidesulfovibrio alaskensis G20
brenda
Politi, J.; Spadavecchia, J.; Fiorentino, G.; Antonucci, I.; De Stefano, L.
Arsenate reductase from Thermus thermophilus conjugated to polyethylene glycol-stabilized gold nanospheres allow trace sensing and speciation of arsenic ions
J. R. Soc. Interface
13
20160629
2016
Thermus thermophilus
brenda