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Literature summary for 1.20.4.1 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
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
C106G the maximal velocity is approximately half that of the wild type enzyme Escherichia coli
C12S catalytically inactive mutant Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
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
NEM
-
 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
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

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