BRENDA - Enzyme Database show

ArsD residues Cys12, Cys13, and Cys18 form an As(III)-binding site required for arsenic metallochaperone activity

Lin, Y.F.; Yang, J.; Rosen, B.P.; J. Biol. Chem. 282, 16783-16791 (2007)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
7.3.2.7
expression of ArsA and ArsD wild-type and mutants in a Saccharomyces cerevisiae two-hybrid system
Escherichia coli
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
7.3.2.7
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
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
7.3.2.7
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)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
687554
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
?
7.3.2.7
ATP + H2O + arsenite/in
metalloid-binding site MBS1 is involved in metalloid transfer and ArsA activation
687554
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
?
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
7.3.2.7
37
-
assay at
Escherichia coli
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
7.3.2.7
expression of ArsA and ArsD wild-type and mutants in a Saccharomyces cerevisiae two-hybrid system
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
7.3.2.7
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
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
687554
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
?
7.3.2.7
ATP + H2O + arsenite/in
metalloid-binding site MBS1 is involved in metalloid transfer and ArsA activation
687554
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
?
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
7.3.2.7
37
-
assay at
Escherichia coli