EC - Arsenate reductase (glutathione/glutaredoxin)

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IntEnz Enzyme Nomenclature


Accepted name:
arsenate reductase (glutathione/glutaredoxin)
Other names:
ArsC [ambiguous]
arsenate:glutaredoxin oxidoreductase
arsenate reductase (glutaredoxin)
Systematic name:
arsenate:glutathione/glutaredoxin oxidoreductase




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).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UM-BBD , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008794
UniProtKB/Swiss-Prot: (19) [show] [UniProt]


  1. Gladysheva, T., Liu, J.Y. and Rosen, B.P.
    His-8 lowers the pKa of the essential Cys-12 residue of the ArsC arsenate reductase of plasmid R773.
    J. Biol. Chem. 271 : 33256-33260 (1996). [PMID: 8969183]
  2. Gladysheva, T.B., Oden, K.L. and Rosen, B.P.
    Properties of the arsenate reductase of plasmid R773.
    Biochemistry 33 : 7288-7293 (1994). [PMID: 8003492]
  3. Holmgren, A. and Aslund, F.
    Methods Enzymol. 252 : 283-292 (1995). [PMID: 7476363]
  4. Krafft, T. and Macy, J.M.
    Purification and characterization of the respiratory arsenate reductase of Chrysiogenes arsenatis.
    Eur. J. Biochem. 255 : 647-653 (1998). [PMID: 9738904]
  5. Martin, J.L.
    Thioredoxin - a fold for all reasons.
    Structure 3 : 245-250 (1995). [PMID: 7788290]
  6. Radabaugh, T.R. and Aposhian, H.V.
    Enzymatic reduction of arsenic compounds in mammalian systems: reduction of arsenate to arsenite by human liver arsenate reductase.
    Chem. Res. Toxicol. 13 : 26-30 (2000). [PMID: 10649963]
  7. Sato, T. and Kobayashi, Y.
    The ars operon in the skin element of Bacillus subtilis confers resistance to arsenate and arsenite.
    J. Bacteriol. 180 : 1655-1661 (1998). [PMID: 9537360]
  8. Shi, J., Vlamis-Gardikas, V., Aslund, F., Holmgren, A. and Rosen, B.P.
    Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction.
    J. Biol. Chem. 274 : 36039-36042 (1999). [PMID: 10593884]
  9. Mukhopadhyay, R., Rosen, B. P.
    Arsenate reductases in prokaryotes and eukaryotes.
    Environ. Health Perspect. 110 Suppl 5 : 745-748 (2002). [PMID: 12426124]
  10. Messens, J., Silver, S.
    Arsenate reduction: thiol cascade chemistry with convergent evolution.
    J. Mol. Biol. 362 : 1-17 (2006). [PMID: 16905151]

[EC created 2000 as EC, transferred 2001 to EC, modified 2015, modified 2019, modified 2020]