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Literature summary for 7.3.2.7 extracted from

  • Yang, J.; Rawat, S.; Stemmler, T.L.; Rosen, B.P.
    Arsenic binding and transfer by the ArsD As(III) metallochaperone (2010), Biochemistry, 49, 3658-3666.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.3.2.7

Activating Compound

Activating Compound Comment Organism Structure
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
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + antimonite/in Escherichia coli
-
 ADP + phosphate + antimonite/out
-
 ?
ATP + H2O + arsenite/in Escherichia coli
-
 ADP + phosphate + arsenite/out
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 ArsAB pump is encoded in arsRDABC operon on plasmid R773
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + antimonite/in
-
 Escherichia coli ADP + phosphate + antimonite/out
-
 ?
ATP + H2O + arsenite/in
-
 Escherichia coli ADP + phosphate + arsenite/out
-
 ?
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 Escherichia coli ADP + phosphate + arsenite/out
-
 ?
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 Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
ArsAB pump
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 ATPase assay at Escherichia coli

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
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

General Information Comment Organism
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