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Literature summary extracted from

  • Ruan, X.; Bhattacharjee, H.; Rosen, B.P.
    Characterization of the metalloactivation domain of an arsenite/antimonite resistance pump (2008), Mol. Microbiol., 67, 392-402.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
7.3.2.7 C113A/C422A site-directed mutagenesis, the mutant lacks As(III) activation activity compared to the wild-type enzyme Escherichia coli
7.3.2.7 C172A site-directed mutagenesis, an ArsA mutant, the mutant shows reduced affinity for Sb(III) compared to the wild-type enzyme Escherichia coli
7.3.2.7 C172A/H453A site-directed mutagenesis, the ArsA double mutant exhibits significantly decreased affinity for Sb(III) Escherichia coli
7.3.2.7 H148A/S420A site-directed mutagenesis, the mutant exhibits a half-maximal stimulation similar to that of the wild-type enzyme 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 the ArsAB extrusion pump confers resistance to the toxic trivalent metalloids arsenite [As(III)] and antimonite [Sb(III)], overview ADP + phosphate + arsenite/out
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Organism

EC Number Organism UniProt Comment Textmining
7.3.2.7 Escherichia coli P08690 the enzyme is encoded by the ars operon of 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 the ArsAB extrusion pump confers resistance to the toxic trivalent metalloids arsenite [As(III)] and antimonite [Sb(III)], overview Escherichia coli ADP + phosphate + arsenite/out
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7.3.2.7 ATP + H2O + arsenite/in ArsA ATPase, the catalytic subunit of the pump, has two homologous halves, A1 and A2, and at the interface of these two halves are two nucleotide-binding domains and a metalloid-binding domain, Cys113 and Cys422 form a high-affinity metalloid binding site. Two other metalloid atoms are bound, one liganded to Cys172 and His453, and the other liganded to His148 and Ser420, but there is only a single high-affinity metalloid binding site in ArsA, and second that Cys172 controls the affinity of this site for metalloid and hence the efficiency of metalloactivation of the ArsAB efflux pump, metalloid binding site MBS structure and mechanism, overview Escherichia coli ADP + phosphate + arsenite/out
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Subunits

EC Number Subunits Comment Organism
7.3.2.7 More ArsA ATPase, the catalytic subunit of the pump, has two homologous halves, A1 and A2, and at the interface of these two halves are two nucleotide-binding domains and a metalloid-binding domain, Cys113 and Cys422 form a high-affinity metalloid binding site. There is only a single high-affinity metalloid binding site in ArsA, and second that Cys172 controls the affinity of this site for metalloid and hence the efficiency of metalloactivation of the ArsAB efflux pump Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
7.3.2.7 ArsAB extrusion pump
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 Escherichia coli
7.3.2.7 arsenite/antimonite resistance pump
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 Escherichia coli