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Literature summary for 1.20.4.1 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
Search for more literature for 1.20.4.1

Activating Compound

Activating Compound Comment Organism Structure
GSH required Escherichia coli

Protein Variants

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

Natural Substrates/ Products (Substrates)

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

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

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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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arsenate + reduced glutaredoxin the enzyme is involved in bacterial arsenic resistance Escherichia coli arsenite + oxidized glutaredoxin
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