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Information on EC 1.20.4.4 - arsenate reductase (thioredoxin)
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1.20.4.4 arsenate reductase (thioredoxin)IUBMB Comments
The enzyme, characterized in bacteria of the Firmicutes phylum, is specific for thioredoxin . It has no activity with glutaredoxin [cf. EC 1.20.4.1, arsenate reductase (glutaredoxin)]. Although the arsenite formed is more toxic than arsenate, it can be extruded from some bacteria by EC 3.6.3.16, arsenite-transporting ATPase; in other organisms, arsenite can be methylated by EC 2.1.1.137, arsenite methyltransferase, in a pathway that produces non-toxic organoarsenical compounds. The enzyme also has the activity of EC 3.1.3.48, protein-tyrosine-phosphatase .
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
arsc3, sa_arsc, pi258 arsenate reductase, thioredoxin-coupled arsenate reductase, bs_arsc, arsc1', thioredoxin-arsenate reductase complex, trx-coupled arsenate reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ARS
ArsC
ArsC1
ArsC1 is related to thioredoxin-dependent arsenate reductases
ArsC1'
ArsC3
arsenate reductase
Strop634
-
gene name, protein comprises two domains an aquaglyceroporin-derived N-terminal channel-like part fused to a C-terminal enzyme domain with similarity to ArsC arsenate reductase, protein also shows minor phosphotyrosine phosphatase activity
thioredoxin-coupled arsenate reductase
Trx-coupled arsenate reductase
ArsC3
ArsC3 is related to thioredoxin-dependent arsenate reductases but ArsC3 lacks the two distal catalytic cysteine residues of this class of enzymes
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
arsenate + thioredoxin = arsenite + thioredoxin disulfide + H2O
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
thioredoxin:arsenate oxidoreductase
The enzyme, characterized in bacteria of the Firmicutes phylum, is specific for thioredoxin [1]. It has no activity with glutaredoxin [cf. EC 1.20.4.1, arsenate reductase (glutaredoxin)]. Although the arsenite formed is more toxic than arsenate, it can be extruded from some bacteria by EC 3.6.3.16, arsenite-transporting ATPase; in other organisms, arsenite can be methylated by EC 2.1.1.137, arsenite methyltransferase, in a pathway that produces non-toxic organoarsenical compounds. The enzyme also has the activity of EC 3.1.3.48, protein-tyrosine-phosphatase [3].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
?
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
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
?
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
?
-
enzyme additionally exhibits weak phosphatase activity
-
-
-
additional information
?
-
-
enzyme additionally exhibits weak phosphatase activity
-
-
-
additional information
?
-
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
enzyme additionally exhibits weak phosphatase activity
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
arsenate + thioredoxin
arsenite + thioredoxin disulfide + H2O
P0A006
-
-
-
?
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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thioredoxin
-
interaction between thioredoxin and the enzyme pI258 arsenate reductase. Thioredoxin converts oxidized ArsC back towards its initial reduced state
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
-
additional information
-
ArsC couples to thioredoxin, thioredoxin reductase, and NADPH to be enzymatically active
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
iodoacetate
sulfhydryl inhibitors N-ethylmaleimide -and iodoacetate inhibit arsenate reductase activity by 80% in crude cell-free preparations and by 90% with purified ArsC protein
N-ethylmaleimide
sulfhydryl inhibitors N-ethylmaleimide -and iodoacetate inhibit arsenate reductase activity by 80% in crude cell-free preparations and by 90% with purified ArsC protein
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
stimulates ArsC-dependent arsenate reduction, but not 2-mercaptoethanol or reduced glutathione
thioredoxin
and dithiothreitol are needed for arsenate reduction
additional information
-
mechanism by which potassium and tetrahedral oxyanions affect catalysis within the Trx-coupled family of arsenate reductases
-
additional information
-
mechanism by which potassium and tetrahedral oxyanions affect catalysis within the Trx-coupled family of arsenate reductases
-
additional information
reduction of arsenate to arsenite is dependent on the presence of the arsC gene and the extent of reduction depended also upon the presence of arsB. The arsC-deletion mutant plasmids pGJ106 and pGJ107 confer no more arsenate reduction activity than does the vector plasmid pSK265. Without intact arsB (plasmids pGJ105 and pGJ109) somewhat less arsenite is found
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.047
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
0.123
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
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.061
arsenate
-
C15A ArsC mutant, at 2 microM AsO43-; pH 7.5, 37°C, mutant enzyme C15A, at 0.002 mM arsenate
0.075
arsenate
-
pH 7.5, 37°C, wild-type enzyme, at 0.002 mM arsenate; wild-type ArsC, at 2 microM AsO43-
0.08
arsenate
-
C15A ArsC mutant, at 10 mM AsO43-; pH 7.5, 37°C, mutant enzyme C15A, at 10 mM arsenate
0.165
arsenate
-
pH 7.5, 37°C, wild-type enzyme, at 10 mM arsenate; wild-type ArsC, at 10 mM AsO43-
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
-
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; 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
2.9
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
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
3.65
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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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9.5
ArsC arsenate reductase activity is decreased >80% at pH 6.3 but is stable in the pH range 7.0-9.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme additionally shows low phosphates activity
UniProt
brenda
enzyme additionally shows low phosphates activity
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
ArsC3 together with ArsC1 is able to rescue the arsenate sensitivity phenotype of Escherichia coli mutant AW3110; 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; Salinispora tropica Strop634 deletion strains are highly sensitive to arsenate exposure
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
ArsC1 functions as an arsenate reductase required for As(V) detoxification; 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); ArsC3 functions as arsenate reductase required for As(V) detoxification; 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; confers arsenate resistance in Salinispora tropica
physiological function
-
isoform ArsC3 is functional and able to confer arsenate resistance to Escherichia coli
physiological function
-
isoform ArsC3 is functional and able to confer arsenate resistance to Escherichia coli
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Bacillus subtilis (strain 168)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14400
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
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
14810
16000
-
1 * 16010, calculated, 1 * 16000, SDS-PAGE, 1 * 16008, ESI-microTOF
16008
-
1 * 16010, calculated, 1 * 16000, SDS-PAGE, 1 * 16008, ESI-microTOF
16010
-
1 * 16010, calculated, 1 * 16000, SDS-PAGE, 1 * 16008, ESI-microTOF
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
?
-
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
monomer
-
1 * 16010, calculated, 1 * 16000, SDS-PAGE, 1 * 16008, ESI-microTOF
monomer
-
1 * 16010, calculated, 1 * 16000, SDS-PAGE, 1 * 16008, ESI-microTOF
-
monomer
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
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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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C10S/C15A/C82S
-
mutant in complex with the thioredoxin C32S mutant. Solve the structure of the Trx-ArsC complex by NMR spectroscopy
C10A
C10S/C15A
C10S/C15A/C82S
C10S/C15A/C89L
-
mutant, determination of the redox potential of the Cys82-Cys89 redox couple
C15A
C82A
C82S
-
inactive mutant enzyme; site-directed mutagenesis, mutation of Cys 10, 82, and 89 leads to redox-inactive enzymes
C89A
C7S
additional information
C10A
-
inactive mutant enzyme; site-directed mutagenesis, mutation of Cys 10, 82, and 89 leads to redox-inactive enzymes
C10S/C15A/C82S
-
site-directed mutagenesis, triple mutant, structure very similar to that of the reduced form of wild-type ArsC
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
C15A
-
as compared to wild-type enzyme the affinity is reduced ba a factor of 2; site-directed mutagenesis, only ArsC wild type and ArsC C15A show enzymatic activity
C82A
-
site-directed mutagenesis, mutation of Cys 10, 82, and 89 leads to redox-inactive enzymes
C89A
-
inactive mutant enzyme; site-directed mutagenesis, mutation of Cys 10, 82, and 89 leads to redox-inactive enzymes
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
-
essential cysteinyl residues and redox couple in arsenate reductase are identified by a combination of site-specific mutagenesis and endoprotease-digest mass spectroscopy analysis
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9.5
ArsC arsenate reductase activity is decreased >80% at pH 6.3 but is stable in the pH range 7.0-9.5
706565
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
heat-stable, surviving 2 min heating at 80°C
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
; wild-type ArsC and the Cys mutants, gel filtration more than 97% pure
-
C10S/C15A/C89L mutant and C10S/C15A/C82S mutant purified by Ni2+-NTA Superflow
-
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
C10S/C15A/C89L mutant and C10S/C15A/C82S mutant expressed in Escherichia coli
-
expressed in Escherichia coli
expressed 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
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expression in Escherichia coli
overproduced in Escherichia coli K38(pGP1-2)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is 4fold increased in presence of arsenate in the growth medium
isooform ArsC1' is constitutively expressed at low levels using its own promoter site. It reduces arsenate to arsenite that can then induce the expression of isoforms ArsC1 and ArsC2
expression is 4fold increased in presence of arsenate in the growth medium
expression is 4fold increased in presence of arsenate in the growth medium
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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isooform ArsC1' is constitutively expressed at low levels using its own promoter site. It reduces arsenate to arsenite that can then induce the expression of isoforms ArsC1 and ArsC2
isooform ArsC1' is constitutively expressed at low levels using its own promoter site. It reduces arsenate to arsenite that can then induce the expression of isoforms ArsC1 and ArsC2
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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, Bacillus subtilis (P45947)
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
Bacillus subtilis, Bacillus subtilis (P45947), Staphylococcus aureus (P0A006), Staphylococcus aureus
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
Desulfovibrio alaskensis, Desulfovibrio 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
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