BRENDA - Enzyme Database show
show all sequences of 7.3.2.7

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
Amino acid exchange
Commentary
Organism
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
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
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
Localization
Commentary
Organism
GeneOntology No.
Textmining
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
As3+
As(III)-stimulated ATPase activity
Alkaliphilus metalliredigens
Sb3+
Sb(III)-stimulated ATPase activity 4-8fold
Alkaliphilus metalliredigens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + H2O + antimonite/in
Alkaliphilus metalliredigens
-
ADP + phosphate + antimonite/out
-
-
-
ATP + H2O + arsenite/in
Alkaliphilus metalliredigens
-
ADP + phosphate + arsenite/out
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
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)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + H2O + antimonite/in
-
719496
Alkaliphilus metalliredigens
ADP + phosphate + antimonite/out
-
-
-
-
ATP + H2O + arsenite/in
-
719496
Alkaliphilus metalliredigens
ADP + phosphate + arsenite/out
-
-
-
-
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
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
7.8
-
Alkaliphilus metalliredigens
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
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
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
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)
Localization
Commentary
Organism
GeneOntology No.
Textmining
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
As3+
As(III)-stimulated ATPase activity
Alkaliphilus metalliredigens
Sb3+
Sb(III)-stimulated ATPase activity 4-8fold
Alkaliphilus metalliredigens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + H2O + antimonite/in
Alkaliphilus metalliredigens
-
ADP + phosphate + antimonite/out
-
-
-
ATP + H2O + arsenite/in
Alkaliphilus metalliredigens
-
ADP + phosphate + arsenite/out
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + H2O + antimonite/in
-
719496
Alkaliphilus metalliredigens
ADP + phosphate + antimonite/out
-
-
-
-
ATP + H2O + arsenite/in
-
719496
Alkaliphilus metalliredigens
ADP + phosphate + arsenite/out
-
-
-
-
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)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
7.8
-
Alkaliphilus metalliredigens
General Information
General Information
Commentary
Organism
additional information
the Cys108 of AmArsA1 and Cys120 of AmArsA2 form part of the metalloid binding domain
Alkaliphilus metalliredigens
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)
General Information
Commentary
Organism
additional information
the Cys108 of AmArsA1 and Cys120 of AmArsA2 form part of the metalloid binding domain
Alkaliphilus metalliredigens
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
Other publictions for EC 7.3.2.7
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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1
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719496
Fu
Biochemical characterization o ...
Alkaliphilus metalliredigens
FEBS Lett.
584
3089-3094
2010
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2008
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Escherichia coli
Biochemistry
47
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2008
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Pseudomonas putida
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Tseng
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Caenorhabditis elegans
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2007
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687482
Lin
ArsD: an As(III) metallochaper ...
Escherichia coli
J. Bioenerg. Biomembr.
39
453-458
2007
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687554
Lin
ArsD residues Cys12, Cys13, an ...
Escherichia coli
J. Biol. Chem.
282
16783-16791
2007
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