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 .
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
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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].
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
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
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
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
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
sulfhydryl inhibitors N-ethylmaleimide -and iodoacetate inhibit arsenate reductase activity by 80% in crude cell-free preparations and by 90% with purified ArsC protein
sulfhydryl inhibitors N-ethylmaleimide -and iodoacetate inhibit arsenate reductase activity by 80% in crude cell-free preparations and by 90% with purified ArsC protein
arsenite, tellurite, and antimonite [Sb(III)] are inhibitors for NADPH oxidation; the substrate, arsenate, is not inhibitory at concentrations up to 40 mM
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
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
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
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
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: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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 Na2SO4, 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
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
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
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
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
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
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
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)
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
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
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
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
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
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
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
essential cysteinyl residues and redox couple in arsenate reductase are identified by a combination of site-specific mutagenesis and endoprotease-digest mass spectroscopy analysis
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
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
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
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
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