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Literature summary extracted from

  • Lin, Y.F.; Yang, J.; Rosen, B.P.
    ArsD residues Cys12, Cys13, and Cys18 form an As(III)-binding site required for arsenic metallochaperone activity (2007), J. Biol. Chem., 282, 16783-16791.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.3.2.7 expression of ArsA and ArsD wild-type and mutants in a Saccharomyces cerevisiae two-hybrid system Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.3.2.7 ATP + H2O + arsenite/in Escherichia coli ArsD residues Cys12, Cys13, and Cys18, but not Cys112, Cys113, Cys119, or Cys120, from an As(III)-binding site are required for arsenic metallochaperone activity, ArsD is a metallochaperone that delivers As(III) to ArsA, increasing its affinity for As(III), thus conferring resistance to environmental concentrations of arsenic, ArsD mutants with alanines substituting for Cys112, Cys113, Cys119, or Cys120 individually or in pairs or truncations lacking the vicinal pairs retain the ability to interact with ArsA and to activate its ATPase activity, mutational interaction analysis, overview ADP + phosphate + arsenite/out
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 ?

Organism

EC Number Organism UniProt Comment Textmining
7.3.2.7 Escherichia coli
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 strains JM109 and BL21, ArsA ATPase is the catalytic subunit of the ArsAB pump encoded by the arsRDABC operon of Escherichia coli plasmid R773
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.3.2.7 ATP + H2O + arsenite/in ArsD residues Cys12, Cys13, and Cys18, but not Cys112, Cys113, Cys119, or Cys120, from an As(III)-binding site are required for arsenic metallochaperone activity, ArsD is a metallochaperone that delivers As(III) to ArsA, increasing its affinity for As(III), thus conferring resistance to environmental concentrations of arsenic, ArsD mutants with alanines substituting for Cys112, Cys113, Cys119, or Cys120 individually or in pairs or truncations lacking the vicinal pairs retain the ability to interact with ArsA and to activate its ATPase activity, mutational interaction analysis, overview Escherichia coli ADP + phosphate + arsenite/out
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 ?
7.3.2.7 ATP + H2O + arsenite/in metalloid-binding site MBS1 is involved in metalloid transfer and ArsA activation Escherichia coli ADP + phosphate + arsenite/out
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 ?

Synonyms

EC Number Synonyms Comment Organism
7.3.2.7 ARSA
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 Escherichia coli
7.3.2.7 ArsA ATPase
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 Escherichia coli
7.3.2.7 ArsAB pump
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 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
7.3.2.7 37
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 assay at Escherichia coli