BRENDA - Enzyme Database show

The ArsD As(III) metallochaperone

Ajees, A.A.; Yang, J.; Rosen, B.P.; Biometals 24, 391-399 (2011)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
7.3.2.7
ArsD
ArsD is an arsenic chaperone for ArsA. ArsD transfers As(III) to ArsA and increases the affinity of ArsA for As(III). Cys12, Cys13 and Cys18 in ArsD form a three sulfur-coordinated As(III) binding site that is essential for metallochaperone activity, Interaction between ArsD and ArsA, ArsD function, overview
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 + antimonite/in
Escherichia coli
-
ADP + phosphate + antimonite/out
-
-
-
7.3.2.7
ATP + H2O + arsenite/in
Escherichia coli
-
ADP + phosphate + arsenite/out
-
-
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
7.3.2.7
Escherichia coli
-
ArsAB pump is encoded in arsRDABC operon on 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 + antimonite/in
-
719037
Escherichia coli
ADP + phosphate + antimonite/out
-
-
-
-
7.3.2.7
ATP + H2O + arsenite/in
-
719037
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
-
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
7.3.2.7
ArsD
ArsD is an arsenic chaperone for ArsA. ArsD transfers As(III) to ArsA and increases the affinity of ArsA for As(III). Cys12, Cys13 and Cys18 in ArsD form a three sulfur-coordinated As(III) binding site that is essential for metallochaperone activity, Interaction between ArsD and ArsA, ArsD function, overview
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 + antimonite/in
Escherichia coli
-
ADP + phosphate + antimonite/out
-
-
-
7.3.2.7
ATP + H2O + arsenite/in
Escherichia coli
-
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 + antimonite/in
-
719037
Escherichia coli
ADP + phosphate + antimonite/out
-
-
-
-
7.3.2.7
ATP + H2O + arsenite/in
-
719037
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
-
General Information
EC Number
General Information
Commentary
Organism
7.3.2.7
physiological function
ArsA is an ATPase that is the catalytic subunit of the ArsAB As(III) extrusion pump, and ArsD is an arsenic chaperone for ArsA. ArsD transfers As(III) to ArsA and increases the affinity of ArsA for As(III), allowing resistance to environmental concentrations of arsenic. ATP hydrolysis by ArsA is required for transfer of As(III) from ArsD to ArsA, suggesting that transfer occurs with a conformation of ArsA that transiently forms during the catalytic cycle. Docking of ArsD with ArsA, modeling and mechanism, detailed overview. Cysteine-rich metalloid binding sites of ArsD and ArsA come close to each other during interaction, ArsD interacts with nucleotide-bound form. The interface with ArsA involves one surface of alpha1 helix and metalloid binding site of ArsD. ArsB is a As(OH)3/H+ antiporter that extrudes As(III), conferring resistance
Escherichia coli
General Information (protein specific)
EC Number
General Information
Commentary
Organism
7.3.2.7
physiological function
ArsA is an ATPase that is the catalytic subunit of the ArsAB As(III) extrusion pump, and ArsD is an arsenic chaperone for ArsA. ArsD transfers As(III) to ArsA and increases the affinity of ArsA for As(III), allowing resistance to environmental concentrations of arsenic. ATP hydrolysis by ArsA is required for transfer of As(III) from ArsD to ArsA, suggesting that transfer occurs with a conformation of ArsA that transiently forms during the catalytic cycle. Docking of ArsD with ArsA, modeling and mechanism, detailed overview. Cysteine-rich metalloid binding sites of ArsD and ArsA come close to each other during interaction, ArsD interacts with nucleotide-bound form. The interface with ArsA involves one surface of alpha1 helix and metalloid binding site of ArsD. ArsB is a As(OH)3/H+ antiporter that extrudes As(III), conferring resistance
Escherichia coli