EC 1.20.4.1 - Arsenate reductase (glutaredoxin)

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IntEnz Enzyme Nomenclature
EC 1.20.4.1

Names

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

Reaction

Cofactor

Comments:

A molybdoenzyme. The enzyme is part of a system for detoxifying arsenate. Although the arsenite formed is more toxic than arsenate, it can be extruded from some bacteria by EC 3.6.3.16, arsenite-transporting ATPase; in other organisms, arsenite can be methylated by EC 2.1.1.137, arsenite methyltransferase, in a pathway that produces non-toxic organoarsenical compounds. cf. EC 1.20.4.4, arsenate reductase (thioredoxin).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UM-BBD , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008794
UniProtKB/Swiss-Prot: (18) [show] [UniProt]

References

  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: 13460837]
  3. Holmgren, A. and Aslund, F.
    Glutaredoxin.
    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: 9246257]
  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: 7645648]
  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]

[EC 1.20.4.1 created 2000 as EC 1.97.1.5, transferred 2001 to EC 1.20.4.1, modified 2015]