Literature summary for 7.3.2.7 extracted from

Zhou, T.; Rosen, B.P.
Tryptophan fluorescence reports nucleotide-induced conformational changes in a domain of the ArsA ATPase (1997), J. Biol. Chem., 272, 19731-19737.

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	from plasmid R773	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O + arsenite/in	-	Escherichia coli	ADP + phosphate + arsenite/out	-	?
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	Escherichia coli	?	-	?

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Release 2023.1 (January 2023)