Arsenate reductase (glutaredoxin)

arsenate + glutaredoxin $rightleftharpoons$ arsenite + glutaredoxin disulfide + H₂O

Thus, the two substrates of this enzyme are arsenate and glutaredoxin, whereas its 3 products are arsenite, glutaredoxin disulfide, and H₂O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on phosphorus or arsenic in donor with disulfide as acceptor. The systematic name of this enzyme class is glutharedoxin:arsenate oxidoreductase.

Structural studies

As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , and .

References

• Gladysheva T, Liu J, Rosen BP "His-8 lowers the pKa of the essential Cys-12 residue of the ArsC arsenate reductase of plasmid R773". J. Biol. Chem. 271 33256–60.
• Gladysheva TB, Oden KL, Rosen BP "Properties of the arsenate reductase of plasmid R773". Biochemistry. 33 7288–93.
• Holmgren A, Aslund F "Glutaredoxin". Methods. Enzymol. 252 283–92.
• Silver S "Arsenate reductase of Staphylococcus aureus plasmid PI258". Biochemistry 33 7294–7299.
• Krafft T, Macy JM "Purification and characterization of the respiratory arsenate reductase of Chrysiogenes arsenatis". Eur. J. Biochem. 255 647–53.
• Martin JL "Thioredoxin--a fold for all reasons". Structure. 3 245–50.
• Messens J, Hayburn G, Desmyter A, Laus G, Wyns L "The essential catalytic redox couple in arsenate reductase from Staphylococcus aureus". Biochemistry. 38 16857–65.
• Radabaugh TR, Aposhian HV "Enzymatic reduction of arsenic compounds in mammalian systems: reduction of arsenate to arsenite by human liver arsenate reductase". Chem. Res. Toxicol. 13 26–30.
• Sato T, Kobayashi Y "The ars operon in the skin element of Bacillus subtilis confers resistance to arsenate and arsenite". J. Bacteriol. 180 1655–61.
• Shi J, Vlamis-Gardikas A, Aslund F, Holmgren A, Rosen BP "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 36039–42.

External links

Gene Ontology (GO) codes