BRENDA - Enzyme Database show

Asp45 is a Mg2+ ligand in the ArsA ATPase

Zhou, T.; Rosen, B.P.; J. Biol. Chem. 274, 13854-13858 (1999)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
7.3.2.7
antimonite
allosteric activation
Escherichia coli
7.3.2.7
arsenite
allosteric activation
Escherichia coli
Engineering
EC Number
Amino acid exchange
Commentary
Organism
7.3.2.7
D45A
mutant of ArsA, the catalytic subunit of the pump. Inactive enzyme. ATP and Sb(III) synergistically protect wild type ArsA catalytic subunit from trypsin digestion. Subsequent addition of Mg2+ increases trypsin digestion. Mutant D45N and D45A remain protected by ATP and Sb(III) but lose the Mg2+ effect
Escherichia coli
7.3.2.7
D45E
approximately 5% of the wild type activity with about a 5fold decrease in affinity for Mg2+. ATP and Sb(III) synergistically protect wild type ArsA catalytic subunit from trypsin digestion. Subsequent addition of Mg2+ increases trypsin digestion, D45E exhibits an lower Mg2+ response
Escherichia coli
7.3.2.7
D45N
mutant of Ars A, the catalytic subunit of the pump. Inactive enzyme. ATP and Sb(III) synergistically protect wild type ArsA catalytic subunit from trypsin digestion. Subsequent addition of Mg2+ increases trypsin digestion. Mutant D45N and D45A remain protected by ATP and Sb(III) but lose the Mg2+ effect
Escherichia coli
General Stability
EC Number
General Stability
Organism
7.3.2.7
ATP and Sb(III) synergistically protect wild type ArsA catalytic subunit from trypsin digestion. Subsequent addition of Mg2+ increases trypsin digestion. Mutant D45N and D45A remain protected by ATP and Sb(III) but lose the Mg2+ effect. D45E exhibits an intermediate Mg2+ response
Escherichia coli
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
7.3.2.7
Mg2+
Asp45 of ArsA, the catalytic subunit of the pump is a Mg2+ ligand; required
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
-
ADP + phosphate + arsenite/out
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
7.3.2.7
Escherichia coli
-
-
-
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
-
210282
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
?
7.3.2.7
ATP + H2O + arsenite/in
-
210282
Escherichia coli
ADP + phosphate + arsenite/out
-
210282
Escherichia coli
?
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
7.3.2.7
antimonite
allosteric activation
Escherichia coli
7.3.2.7
arsenite
allosteric activation
Escherichia coli
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
7.3.2.7
D45A
mutant of ArsA, the catalytic subunit of the pump. Inactive enzyme. ATP and Sb(III) synergistically protect wild type ArsA catalytic subunit from trypsin digestion. Subsequent addition of Mg2+ increases trypsin digestion. Mutant D45N and D45A remain protected by ATP and Sb(III) but lose the Mg2+ effect
Escherichia coli
7.3.2.7
D45E
approximately 5% of the wild type activity with about a 5fold decrease in affinity for Mg2+. ATP and Sb(III) synergistically protect wild type ArsA catalytic subunit from trypsin digestion. Subsequent addition of Mg2+ increases trypsin digestion, D45E exhibits an lower Mg2+ response
Escherichia coli
7.3.2.7
D45N
mutant of Ars A, the catalytic subunit of the pump. Inactive enzyme. ATP and Sb(III) synergistically protect wild type ArsA catalytic subunit from trypsin digestion. Subsequent addition of Mg2+ increases trypsin digestion. Mutant D45N and D45A remain protected by ATP and Sb(III) but lose the Mg2+ effect
Escherichia coli
General Stability (protein specific)
EC Number
General Stability
Organism
7.3.2.7
ATP and Sb(III) synergistically protect wild type ArsA catalytic subunit from trypsin digestion. Subsequent addition of Mg2+ increases trypsin digestion. Mutant D45N and D45A remain protected by ATP and Sb(III) but lose the Mg2+ effect. D45E exhibits an intermediate Mg2+ response
Escherichia coli
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
7.3.2.7
Mg2+
Asp45 of ArsA, the catalytic subunit of the pump is a Mg2+ ligand; required
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
-
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
-
210282
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
?
7.3.2.7
ATP + H2O + arsenite/in
-
210282
Escherichia coli
ADP + phosphate + arsenite/out
-
210282
Escherichia coli
?