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Literature summary for 7.3.2.7 extracted from

  • Ye, J.; Ajees, A.A.; Yang, J.; Rosen, B.P.
    The 1.4 A crystal structure of the ArsD arsenic metallochaperone provides insights into its interaction with the ArsA ATPase (2010), Biochemistry, 49, 5206-5212.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
ArsD arsenic metallochaperone ArsD delivers As(III) to the ArsA ATPase, the catalytic subunit of the ArsAB pump. ArsD binds one arsenic per monomer coordinated with the three sulfur atoms of Cys12, Cys13 and Cys18, modeling of ArsD with and without bound As(III), overview. For analysis of metallo chaperone activity a recombinant truncated form, ArsD109, is used Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
ArsAB pump
-
Saccharomyces cerevisiae

General Information

General Information Comment Organism
additional information for arsenite transport, metallated ArsD interacts with and transfers As(III) to ArsA during catalysis, when the ATPase cycles between open to closed conformations, structure and ArsD-ArsA interaction analysis, docking of ArsD and ArsA and modeling, overview Saccharomyces cerevisiae