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Literature summary extracted from

  • Liu, J.; Rosen, B.P.
    Ligand interactions of the ArsC arsenate reductase (1997), J. Biol. Chem., 272, 21084-21089.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.20.4.1 GSH required Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.20.4.1 A11W same Km for arsenate as the wild type with maximal velocity approximately half that of the wild type enzyme Escherichia coli
1.20.4.1 A11W/C12S catalytic inactive mutation Escherichia coli
1.20.4.1 Y7W same Km and maximal velocity as the wild type Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.20.4.1 arsenate + reduced glutaredoxin Escherichia coli the enzyme is involved in bacterial arsenic resistance arsenite + oxidized glutaredoxin
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Organism

EC Number Organism UniProt Comment Textmining
1.20.4.1 Escherichia coli
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.20.4.1 arsenate + reduced glutaredoxin the first step of the reaction is the binding of arsenate, followed by the interaction of the enzyme-arsenate complex with GSH. A reaction scheme is hypothesized in which the enzyme forms a mixed disulfide between the Cys-12 thiolate of ArsC and GSH. Glutaredoxin would then be required to resolve the mixed disulfide, regenerating reduced ArsC Escherichia coli arsenite + oxidized glutaredoxin
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1.20.4.1 arsenate + reduced glutaredoxin the enzyme is involved in bacterial arsenic resistance Escherichia coli arsenite + oxidized glutaredoxin
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 ?