BRENDA - Enzyme Database show

An arsenic metallochaperone for an arsenic detoxification pump

Lin, Y.F.; Walmsley, A.R.; Rosen, B.P.; Proc. Natl. Acad. Sci. USA 103, 15617-15622 (2006)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
7.3.2.7
ArsD
encoded in the arsRDABC operon, the dimeric 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 arsenite and antimonite , thus increasing its ATPase activity at lower concentrations of arsenite 60fold, as well as for antimonite, and enhancing the rate of arsenite extrusion rendering cells resistant to environmental concentrations of arsenic, overview, cannot be replaced by DTT
Escherichia coli
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 for interaction analysis, overview
Escherichia coli
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
7.3.2.7
As3+
stimulates
Escherichia coli
7.3.2.7
Mg2+
as MgATP2-
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
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
ADP + phosphate + antimonite/out
-
-
?
7.3.2.7
ATP + H2O + arsenite/in
Escherichia coli
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 arsenite, thus increasing its ATPase activity at lower concentrations of arsenite and enhancing the rate of arsenite extrusion rendering cells resistant to environmental concentrations of arsenic, regulatory mechanism, overview
ADP + phosphate + arsenite/out
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
7.3.2.7
Escherichia coli
-
gene arsA, encoded in the arsRDABC operon
-
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
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
689739
Escherichia coli
ADP + phosphate + antimonite/out
-
-
-
?
7.3.2.7
ATP + H2O + arsenite/in
-
689739
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
?
7.3.2.7
ATP + H2O + arsenite/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 arsenite, thus increasing its ATPase activity at lower concentrations of arsenite and enhancing the rate of arsenite extrusion rendering cells resistant to environmental concentrations of arsenic, regulatory mechanism, overview
689739
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
?
7.3.2.7
additional information
ArsA specifically interacts with ArsD but not with ArsR or ArsC
689739
Escherichia coli
?
-
-
-
-
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
7.3.2.7
ArsD
encoded in the arsRDABC operon, the dimeric 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 arsenite and antimonite , thus increasing its ATPase activity at lower concentrations of arsenite 60fold, as well as for antimonite, and enhancing the rate of arsenite extrusion rendering cells resistant to environmental concentrations of arsenic, overview, cannot be replaced by DTT
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 for interaction analysis, overview
Escherichia coli
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
7.3.2.7
As3+
stimulates
Escherichia coli
7.3.2.7
Mg2+
as MgATP2-
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
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
ADP + phosphate + antimonite/out
-
-
?
7.3.2.7
ATP + H2O + arsenite/in
Escherichia coli
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 arsenite, thus increasing its ATPase activity at lower concentrations of arsenite and enhancing the rate of arsenite extrusion rendering cells resistant to environmental concentrations of arsenic, regulatory mechanism, 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 + 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
689739
Escherichia coli
ADP + phosphate + antimonite/out
-
-
-
?
7.3.2.7
ATP + H2O + arsenite/in
-
689739
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
?
7.3.2.7
ATP + H2O + arsenite/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 arsenite, thus increasing its ATPase activity at lower concentrations of arsenite and enhancing the rate of arsenite extrusion rendering cells resistant to environmental concentrations of arsenic, regulatory mechanism, overview
689739
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
?
7.3.2.7
additional information
ArsA specifically interacts with ArsD but not with ArsR or ArsC
689739
Escherichia coli
?
-
-
-
-