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Literature summary extracted from

  • Liu, J.; Gladysheva, T.B.; Lee, L.; Rosen, B.P.
    Identification of an essential cysteinyl residue in the ArsC arsenate reductase of plasmid R773 (1995), Biochemistry, 34, 13472-13476.
    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 C106G the maximal velocity is approximately half that of the wild type enzyme Escherichia coli
1.20.4.1 C12S catalytically inactive mutant Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.20.4.1 iodoacetate inactivates wild type enzyme and mutant enzyme C106S, in presence of substrate, arsenate, or the competitive inhibitors phosphate or sulfate, the rate of the alkylation is reduced Escherichia coli
1.20.4.1 NEM
-
 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
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.20.4.1 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.20.4.1
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.20.4.1 arsenate + reduced glutaredoxin C12 is located at the active site and is required for catalysis Escherichia coli arsenite + oxidized glutaredoxin
-
 ?
1.20.4.1 arsenate + reduced glutaredoxin the enzyme is involved in bacterial arsenic resistance Escherichia coli arsenite + oxidized glutaredoxin
-
 ?