EC - Arsenate reductase (thioredoxin)

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature


Accepted name:
arsenate reductase (thioredoxin)
Other name:
ArsC [ambiguous]
Systematic name:
arsenate:thioredoxin oxidoreductase



The enzyme, characterized in bacteria of the Firmicutes phylum, is specific for thioredoxin [1]. It has no activity with glutaredoxin [cf. EC, arsenate reductase (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. The enzyme also has the activity of EC, protein-tyrosine-phosphatase [3].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (39) [show] [UniProt]


  1. Ji, G., Garber, E. A., Armes, L. G., Chen, C. M., Fuchs, J. A., Silver, S.
    Arsenate reductase of Staphylococcus aureus plasmid pI258.
    Biochemistry 33 : 7294-7299 (1994). [PMID: 8003493]
  2. Messens, J., Hayburn, G., Desmyter, A., Laus, G., Wyns, L.
    The essential catalytic redox couple in arsenate reductase from Staphylococcus aureus.
    Biochemistry 38 : 16857-16865 (1999). [PMID: 10606519]
  3. Zegers, I., Martins, J. C., Willem, R., Wyns, L., Messens, J.
    Arsenate reductase from S. aureus plasmid pI258 is a phosphatase drafted for redox duty.
    Nat. Struct. Biol. 8 : 843-847 (2001). [PMID: 11573087]
  4. Messens, J., Martins, J. C., Van Belle, K., Brosens, E., Desmyter, A., De Gieter, M., Wieruszeski, J. M., Willem, R., Wyns, L., Zegers, I.
    All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascade.
    Proc. Natl. Acad. Sci. U.S.A. 99 : 8506-8511 (2002). [PMID: 12072565]

[EC created 2015, modified 2019]