BRENDA - Enzyme Database show

Tryptophan fluorescence reports nucleotide-induced conformational changes in a domain of the ArsA ATPase

Zhou, T.; Rosen, B.P.; J. Biol. Chem. 272, 19731-19737 (1997)

Data extracted from this reference:

Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
7.3.2.7
Escherichia coli
-
from plasmid R773
-
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
-
210283
Escherichia coli
ADP + phosphate + arsenite/out
-
210283
Escherichia coli
?
7.3.2.7
additional information
Trp141 moves into a relatively more polar environment upon binding of MgADP- and is a sensitive probe for the binding of the product of hydrolysis. The conserved domain of the ArsA subunit is an energy transduction domain that might be involved in the transmission of energy of ATP hydrolysis to other functions such as transport of arsenite through the ArsB subunit of the oxyanion pump
210283
Escherichia coli
?
-
-
-
-
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
-
210283
Escherichia coli
ADP + phosphate + arsenite/out
-
210283
Escherichia coli
?
7.3.2.7
additional information
Trp141 moves into a relatively more polar environment upon binding of MgADP- and is a sensitive probe for the binding of the product of hydrolysis. The conserved domain of the ArsA subunit is an energy transduction domain that might be involved in the transmission of energy of ATP hydrolysis to other functions such as transport of arsenite through the ArsB subunit of the oxyanion pump
210283
Escherichia coli
?
-
-
-
-