EC Number   |
Natural Substrates |
|---|
   7.3.2.7 | ATP + H2O + antimonite/in |
- |
| 7.3.2.7 | ATP + H2O + antimonite/in |
the arsenic chaperone ArsD transfers trivalent metalloids to ArsA, the catalytic subunit of an As(III)-Sb(III) efflux pump. Interaction with ArsD increases the affinity of ArsA for antimonite, thus increasing its ATPase activity at lower concentrations of antimonite, regulatory mechanism, overview |
| 7.3.2.7 | ATP + H2O + arsenite/in |
- |
| 7.3.2.7 | ATP + H2O + arsenite/in |
the ars operon confers resistance to arsenite, arsenate and antimonite |
| 7.3.2.7 | ATP + H2O + arsenite/in |
the ars genes are transcribed in the presence of an inducer, arsenite. Segmental differences in stability within the polycistronic transcript are proposed to account for the differential expression of the ars genes |
| 7.3.2.7 | ATP + H2O + arsenite/in |
mechanism of transcriptional regulation by the ArssR repressor and allosteric regulation of the ArsA protein, the catalytic subunit of the pump |
| 7.3.2.7 | ATP + H2O + arsenite/in |
detoxifying system |
| 7.3.2.7 | ATP + H2O + arsenite/in |
ArsA ATPase is the catalytic subunit of the ArsAB pump, ArsD is an arsenic chaperone to the ArsAB pump, transferring the trivalent metalloids As(III) and Sb(III) to the ArsA subunit of the pump thereby increasing the affinity of ArsA for As(III), resulting in increased rates if extrusion and resistance to environmentally relevant concentrations of arsenite |
| 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 |
| 7.3.2.7 | ATP + H2O + arsenite/in |
ASNA-1 , encoding a functional ArsA ATPase, is critical for As(III) and Sb(III) tolerance in the intact organism, the enzyme does not provide resistance to other metals, e.g. Cu2+ or Pb2+, overview |
