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Literature summary 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.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
7.3.2.7 Escherichia coli
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from plasmid R773
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Substrates and Products (Substrate)

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