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Literature summary extracted from

  • Bhattacharjee, H.; Choudhury, R.; Rosen, B.P.
    Role of conserved aspartates in the ArsA ATPase (2008), Biochemistry, 47, 7218-7227.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
7.3.2.7 antimonite activates 10fold the ATPase activity of wild-type ArsA, activation rates of mutants, overview Escherichia coli
7.3.2.7 arsenite activates 3fold the ATPase activity of wild-type ArsA, activation rates of mutants, overview Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.3.2.7 expression of His6-tagged wild-type and mutant ArsA in Escherichia coli strain JM109. At high expression level wild-type ArsA is located in the cytosol, mutants D142A, D142E, and D142N are also found predominantly in the cytosol at similar levels as the wild type, but D447A and D447E proteins are found as insoluble aggregates, while only trace amounts of D447N can be observed in the soluble fraction Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
7.3.2.7 D142A site-directed mutagenesis, the mutant is activated by arsenite and antimonite in a similar amount as the wild-type enzyme Escherichia coli
7.3.2.7 D142E site-directed mutagenesis, the mutant is stronger activated by arsenite and antimonite compared to the wild-type enzyme Escherichia coli
7.3.2.7 D142N site-directed mutagenesis, the mutant is activated by arsenite and antimonite in a similar amount as the wild-type enzyme Escherichia coli
7.3.2.7 D447A site-directed mutagenesis, the mutant is less activated by arsenite and antimonite compared to the wild-type enzyme Escherichia coli
7.3.2.7 D447E site-directed mutagenesis, the mutant is less activated by arsenite and antimonite compared to the wild-type enzyme Escherichia coli
7.3.2.7 D447N site-directed mutagenesis, the near complete insolubility of D447N ArsA precludes its purification and biochemical characterization Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.3.2.7 Trypsin trypsin cleaves the ArsA at Arg290 to produce a 32 kDa A1 fragment that is catalytically inactive and remains stable to trypsin digestion, and a slightly smaller A2 fragment which is digested rapidly. The trypsin digestion pattern is much different when all three ligands, ATP, Sb(III), and Mg2+, are added together, conditions that produce activated catalysis, overview Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.3.2.7 additional information
-
 additional information activation kinetics of wild-type and mutant enzymes, overview Escherichia coli
7.3.2.7 0.035
-
 ATP recombinant wild-type enzyme Escherichia coli
7.3.2.7 0.15
-
 ATP recombinant mutant D142E Escherichia coli
7.3.2.7 0.2
-
 ATP recombinant mutant D447E Escherichia coli
7.3.2.7 0.6
-
 ATP recombinant mutant D447A Escherichia coli
7.3.2.7 0.9
-
 ATP recombinant mutant D142N Escherichia coli
7.3.2.7 1.25
-
 ATP recombinant mutant D142A Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.3.2.7 membrane
-
 Escherichia coli 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.3.2.7 Mg2+ required, Asp142 is involved in Mg2+ binding Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.3.2.7 ATP + H2O + arsenite/in Escherichia coli
-
 ADP + phosphate + arsenite/out
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.3.2.7 Escherichia coli
-
 gene arsA
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.3.2.7 recombinant His6-tagged wild-type and mutant ArsA from Escherichia coli strain JM109 to over 95% homogeneity by nickel affinity chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.3.2.7 ATP + H2O + arsenite/in
-
 Escherichia coli ADP + phosphate + arsenite/out
-
 ?
7.3.2.7 ATP + H2O + arsenite/in Asp142 is involved in Mg2+ binding and also plays a role in signal transduction between the catalytic and activation domains. In contrast, Asp447 is not nearly as critical for Mg2+ binding as Asp142 but appears to be in communication between the metal and catalytic sites Escherichia coli ADP + phosphate + arsenite/out
-
 ?

Subunits

EC Number Subunits Comment Organism
7.3.2.7 More ArsA is composed of two homologous halves A1 and A2, each containing a nucleotide binding domain, and a single metalloid binding or activation domain is located at the interface of the two halves of the protein. The metalloid binding domain is connected to the two nucleotide binding domains through two DTAPTGH sequences, one in A1 and the other in A2. The DTAPTGH sequences are proposed to be involved in information communication between the metal and catalytic sites Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
7.3.2.7 ArsA ATPase
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
7.3.2.7 ATP
-
 Escherichia coli