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Information on EC - arsenate reductase (glutathione/glutaredoxin)

for references in articles please use BRENDA:EC1.20.4.1
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IUBMB Comments
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, arsenite-transporting ATPase; in other organisms, arsenite can be methylated by EC, arsenite methyltransferase, in a pathway that produces non-toxic organoarsenical compounds. cf. EC, arsenate reductase (thioredoxin).
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
arsenate reductase, asv reductase, acr2p, pvgrx5, slr0946, synarsc, all0195, pcacr2, mxan_0575, more
arsenate + glutathione + glutaredoxin = arsenite + a glutaredoxin-glutathione disulfide + H2O
show the reaction diagram