Literature summary for 7.3.2.7 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.

Search for more literature for 7.3.2.7

Cloned(Commentary)

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

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
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	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	strains JM109 and BL21, ArsA ATPase is the catalytic subunit of the ArsAB pump encoded by the arsRDABC operon of Escherichia coli plasmid R773	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	-	?
ATP + H2O + arsenite/in	metalloid-binding site MBS1 is involved in metalloid transfer and ArsA activation	Escherichia coli	ADP + phosphate + arsenite/out	-	?

Synonyms

Synonyms	Comment	Organism
ARSA	-	Escherichia coli
ArsA ATPase	-	Escherichia coli
ArsAB pump	-	Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Escherichia coli

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Release 2023.1 (January 2023)