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Literature summary extracted from

  • Fu, H.L.; Rosen, B.P.; Bhattacharjee, H.
    Biochemical characterization of a novel ArsA ATPase complex from Alkaliphilus metalliredigens QYMF (2010), FEBS Lett., 584, 3089-3094.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
7.3.2.7 C108A alteration of either Cys108 or Cys120 to alanine results in loss of metalloid binding to either pre-mixed or copurified AmArsAs, indicating that the Cys108 of AmArsA1 and Cys120 of AmArsA2 form part of the metalloid binding domain Alkaliphilus metalliredigens
7.3.2.7 C120A alteration of either Cys108 or Cys120 to alanine results in loss of metalloid binding to either pre-mixed or copurified AmArsAs, indicating that the Cys108 of AmArsA1 and Cys120 of AmArsA2 form part of the metalloid binding domain Alkaliphilus metalliredigens
7.3.2.7 additional information heterologous expression of one of the Alkaliphilus metalliredigens ars operons (ars1) confers arsenite but not antimonite resistance to DELTAars Escherichia coli strain AW3110. Only the co-expressed AmArsA1 and AmArsA2 display arsenite or antimonite stimulate ATPase activity, phenotype, overview Alkaliphilus metalliredigens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.3.2.7 As3+ As(III)-stimulated ATPase activity Alkaliphilus metalliredigens
7.3.2.7 Sb3+ Sb(III)-stimulated ATPase activity 4-8fold Alkaliphilus metalliredigens

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 + antimonite/in Alkaliphilus metalliredigens
-
 ADP + phosphate + antimonite/out
-
 ?
7.3.2.7 ATP + H2O + arsenite/in Alkaliphilus metalliredigens
-
 ADP + phosphate + arsenite/out
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.3.2.7 Alkaliphilus metalliredigens
-
 two ars operons, ars1 and ars2, the arsA gene is split in halves, amarsA1 and amarsA2, and, acr3 but not an arsB gene coexists with arsA
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.3.2.7 ATP + H2O + antimonite/in
-
 Alkaliphilus metalliredigens ADP + phosphate + antimonite/out
-
 ?
7.3.2.7 ATP + H2O + arsenite/in
-
 Alkaliphilus metalliredigens ADP + phosphate + arsenite/out
-
 ?
7.3.2.7 additional information the AmArsA1-AmArsA2 complex has metalloid-stimulated ATPase activity. ArsB transports antimonite, while Acr3 does not appear to do so Alkaliphilus metalliredigens ?
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3.2.7 7.5 7.8
-
 Alkaliphilus metalliredigens

General Information

EC Number General Information Comment Organism
7.3.2.7 additional information the Cys108 of AmArsA1 and Cys120 of AmArsA2 form part of the metalloid binding domain Alkaliphilus metalliredigens
7.3.2.7 physiological function AmArsA1-AmArsA2 interaction is needed to form the functional ArsA ATPase. This novel AmArsA1-AmArsA2 complex may provide insight in how it participates with Acr3 in arsenite detoxification. ArsB transports antimonite, while Acr3 does not appear to do so Alkaliphilus metalliredigens