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Literature summary for 7.3.2.7 extracted from

  • Castillo, R.; Saier, M.H.
    Functional promiscuity of homologues of the bacterial ArsA ATPases (2010), Int. J. Microbiol., 2010, 187373.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
ArsD ArsD is a metallochaperone which sequesters arsenite and antimonite and transfers them to the ArsA ATPase increasing the apparent affinity of ArsA for its substrates and lowering the concentration of free As(III) and Sb(III) in the cytosol Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
gene arsA, phylogenetic analysis with detailed analysis of clustering in the superfamily, overview 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
-
genes arsA and arsB
-

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
-
?

Subunits

Subunits Comment Organism
More subunit ArsA exhibuts ATPase activity and subunit ArsB is a 12 alpha-helix transmembrane spanning pump extruding As(III) and Sb(III) Escherichia coli

General Information

General Information Comment Organism
evolution phylogenetic analysis of gene arsA and prokaryotic and eukaryotic ArsA homologues with detailed analysis of clustering in the superfamily, overview Escherichia coli
physiological function subunit ArsA exhibuts ATPase activity and subunit ArsB is a 12 alpha-helix transmembrane spanning pump extruding As(III) and Sb(III). Transport via ArsB can be energized by the pmf or by forming an oxyanion translocating complex with the catalytic ArsA subunit, coupling ATP hydrolysis to efflux Escherichia coli