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Biochemical characterization of a novel ArsA ATPase complex from Alkaliphilus metalliredigens QYMF

Fu, H.L.; Rosen, B.P.; Bhattacharjee, H.; FEBS Lett. 584, 3089-3094 (2010)

Data extracted from this reference:

Engineering
EC Number
Amino acid exchange
Commentary
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
Commentary
Organism
GeneOntology No.
Textmining
Metals/Ions
EC Number
Metals/Ions
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Primary Accession No. (UniProt)
Commentary
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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
7.3.2.7
ATP + H2O + antimonite/in
-
719496
Alkaliphilus metalliredigens
ADP + phosphate + antimonite/out
-
-
-
-
7.3.2.7
ATP + H2O + arsenite/in
-
719496
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
719496
Alkaliphilus metalliredigens
?
-
-
-
-
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3.2.7
7.5
7.8
-
Alkaliphilus metalliredigens
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
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 (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
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) (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
Alkaliphilus metalliredigens
-
ADP + phosphate + antimonite/out
-
-
-
7.3.2.7
ATP + H2O + arsenite/in
Alkaliphilus metalliredigens
-
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
-
719496
Alkaliphilus metalliredigens
ADP + phosphate + antimonite/out
-
-
-
-
7.3.2.7
ATP + H2O + arsenite/in
-
719496
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
719496
Alkaliphilus metalliredigens
?
-
-
-
-
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3.2.7
7.5
7.8
-
Alkaliphilus metalliredigens
General Information
EC Number
General Information
Commentary
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
General Information (protein specific)
EC Number
General Information
Commentary
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