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ENZYME entry: EC

Accepted Name
arsenate reductase (glutathione/glutaredoxin).
Alternative Name(s)
arsenate reductase (glutaredoxin).
Reaction catalysed
[glutaredoxin]-dithiol + arsenate + glutathione + H(+) <=> arsenite + glutathionyl-S-S-[glutaredoxin] + H2O
  • The enzyme is part of a system for detoxifying arsenate.
  • The substrate binds to a catalytic cysteine residue, forming a covalent thiolate--As(V) intermediate.
  • A tertiary intermediate is then formed between the arsenic, the enzyme's cysteine, and a glutathione cysteine.
  • This intermediate is reduced by glutaredoxin, which forms a dithiol with the glutathione, leading to the dissociation of arsenite.
  • Thus reduction of As(V) is mediated by three cysteine residues: one in ArsC, one in glutathione, and one in glutaredoxin.
  • Although the arsenite formed is more toxic than arsenate, it can be extruded from some bacteria by EC; in other organisms, arsenite can be methylated by EC in a pathway that produces non-toxic organoarsenical compounds; cf. EC
  • Formerly EC
PRIAM enzyme-specific profiles1.20.4.1
KEGG Ligand Database for Enzyme Nomenclature1.20.4.1
IUBMB Enzyme Nomenclature1.20.4.1
MEDLINEFind literature relating to
Rhea expert-curated reactions1.20.4.1
Q336V5, ACR21_ORYSJ;  Q10SX6, ACR22_ORYSJ;  P08692, ARSC1_ECOLX;  
P63621, ARSC_NEIMA;  P63622, ARSC_NEIMB;  Q92R44, ARSC_RHIME;  
P0AB97, ARSC_SHIFL;  P74313, ARSC_SYNY3;  P74984, ARSC_YEREN;  

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