BRENDA - Enzyme Database show

Arsenic binding and transfer by the ArsD As(III) metallochaperone

Yang, J.; Rawat, S.; Stemmler, T.L.; Rosen, B.P.; Biochemistry 49, 3658-3666 (2010)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
7.3.2.7
ArsD
a metallochaperone that delivers trivalent metalloids [As(III) or Sb(III)] to the ArsA ATPase, the catalytic subunit of the ArsAB pump. ArsD residues Cys12, Cys13, and Cys18 are involved in the transfer of As(III) to ArsA
Escherichia coli
7.3.2.7
additional information
in vivo, cytosolic As(III) is nearly completely complexed with GSH. GSH greatly increases the rate of binding of As(III) to ArsD, but GSH does not affect the As(III)-stimulated ArsA ATPase activity
Escherichia coli
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
7.3.2.7
ATP + H2O + antimonite/in
Escherichia coli
-
ADP + phosphate + antimonite/out
-
-
-
7.3.2.7
ATP + H2O + arsenite/in
Escherichia coli
-
ADP + phosphate + arsenite/out
-
-
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
7.3.2.7
Escherichia coli
-
ArsAB pump is encoded in arsRDABC operon on plasmid R773
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
7.3.2.7
ATP + H2O + antimonite/in
-
718868
Escherichia coli
ADP + phosphate + antimonite/out
-
-
-
-
7.3.2.7
ATP + H2O + arsenite/in
-
718868
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
-
7.3.2.7
ATP + H2O + arsenite/in
ArsA has a high-affinity metalloid binding site composed of Cys113 and Cys422, and a third residue, Cys172, that participates in high-affinity binding and activation of ATP hydrolysis
718868
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
-
7.3.2.7
additional information
ArsA exhibits a low, basal rate of ATPase activity in the absence of As(III) or Sb(III) and a higher, activated rate in their presence
718868
Escherichia coli
?
-
-
-
-
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
7.3.2.7
37
-
ATPase assay at
Escherichia coli
Temperature Range [°C]
EC Number
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
7.3.2.7
additional information
-
transfer of As(III) from ArsD to ArsA occurs in the presence of MgATP at 23°C but not at 4°C
Escherichia coli
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
7.3.2.7
ArsD
a metallochaperone that delivers trivalent metalloids [As(III) or Sb(III)] to the ArsA ATPase, the catalytic subunit of the ArsAB pump. ArsD residues Cys12, Cys13, and Cys18 are involved in the transfer of As(III) to ArsA
Escherichia coli
7.3.2.7
additional information
in vivo, cytosolic As(III) is nearly completely complexed with GSH. GSH greatly increases the rate of binding of As(III) to ArsD, but GSH does not affect the As(III)-stimulated ArsA ATPase activity
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
7.3.2.7
ATP + H2O + antimonite/in
Escherichia coli
-
ADP + phosphate + antimonite/out
-
-
-
7.3.2.7
ATP + H2O + arsenite/in
Escherichia coli
-
ADP + phosphate + arsenite/out
-
-
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
7.3.2.7
ATP + H2O + antimonite/in
-
718868
Escherichia coli
ADP + phosphate + antimonite/out
-
-
-
-
7.3.2.7
ATP + H2O + arsenite/in
-
718868
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
-
7.3.2.7
ATP + H2O + arsenite/in
ArsA has a high-affinity metalloid binding site composed of Cys113 and Cys422, and a third residue, Cys172, that participates in high-affinity binding and activation of ATP hydrolysis
718868
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
-
7.3.2.7
additional information
ArsA exhibits a low, basal rate of ATPase activity in the absence of As(III) or Sb(III) and a higher, activated rate in their presence
718868
Escherichia coli
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
7.3.2.7
37
-
ATPase assay at
Escherichia coli
Temperature Range [°C] (protein specific)
EC Number
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
7.3.2.7
additional information
-
transfer of As(III) from ArsD to ArsA occurs in the presence of MgATP at 23°C but not at 4°C
Escherichia coli
General Information
EC Number
General Information
Commentary
Organism
7.3.2.7
additional information
ArsD is a metallochaperone that delivers trivalent metalloids [As(III) or Sb(III)] to the ArsA ATPase, the catalytic subunit of the ArsAB pump. ArsD residues Cys12, Cys13, and Cys18 are involved in the transfer of As(III) to ArsA. Transfer of As(III) from ArsD to ArsA occurs in the presence of MgATP, neither MgADP nor MgATP-gamma-S can replace MgATP. Transfer occurs with a conformation of ArsA that transiently forms during the catalytic cycle and not simply to the closed conformation that ArsA adopts when As(III) and MgATP are bound
Escherichia coli
General Information (protein specific)
EC Number
General Information
Commentary
Organism
7.3.2.7
additional information
ArsD is a metallochaperone that delivers trivalent metalloids [As(III) or Sb(III)] to the ArsA ATPase, the catalytic subunit of the ArsAB pump. ArsD residues Cys12, Cys13, and Cys18 are involved in the transfer of As(III) to ArsA. Transfer of As(III) from ArsD to ArsA occurs in the presence of MgATP, neither MgADP nor MgATP-gamma-S can replace MgATP. Transfer occurs with a conformation of ArsA that transiently forms during the catalytic cycle and not simply to the closed conformation that ArsA adopts when As(III) and MgATP are bound
Escherichia coli