Arsenate reductase (glutaredoxin)

Arsenate reductase (glutaredoxin) (EC 1.20.4.1) is an enzyme that catalyzes the chemical reaction

arsenate + glutaredoxin arsenite + glutaredoxin disulfide + H2O
arsenate reductase (glutaredoxin)
Identifiers
EC number1.20.4.1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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

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 glutaredoxin:arsenate oxidoreductase.

Structural studies

As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1RXE, 1RXI, 1S3C, 1S3D, 1SD8, 1SD9, 1SJZ, 1SK0, 1SK1, 1SK2, 1Z2D, and 1Z2E.

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References
    • Gladysheva T, Liu J, Rosen BP (1996). "His-8 lowers the pKa of the essential Cys-12 residue of the ArsC arsenate reductase of plasmid R773". J. Biol. Chem. 271 (52): 33256–60. doi:10.1074/jbc.271.52.33256. PMID 8969183.
    • Gladysheva TB, Oden KL, Rosen BP (1994). "Properties of the arsenate reductase of plasmid R773". Biochemistry. 33 (23): 7288–93. doi:10.1021/bi00189a033. PMID 8003492.
    • Holmgren A, Aslund F (1995). "Glutaredoxin". Methods Enzymol. 252: 283–92. doi:10.1016/0076-6879(95)52031-7. PMID 7476363.
    • Silver S; Garber, Eric A. E.; Armes, L. Gene; Chen, Chih-Ming; Fuchs, James A.; Silver, Simon (1994). "Arsenate reductase of Staphylococcus aureus plasmid PI258". Biochemistry. 33 (23): 7294–7299. doi:10.1021/bi00189a034. PMID 8003493.
    • Krafft T, Macy JM (1998). "Purification and characterization of the respiratory arsenate reductase of Chrysiogenes arsenatis". Eur. J. Biochem. 255 (3): 647–53. doi:10.1046/j.1432-1327.1998.2550647.x. PMID 9738904.
    • Martin JL (1995). "Thioredoxin--a fold for all reasons". Structure. 3 (3): 245–50. doi:10.1016/S0969-2126(01)00154-X. PMID 7788290.
    • Messens J, Hayburn G, Desmyter A, Laus G, Wyns L (1999). "The essential catalytic redox couple in arsenate reductase from Staphylococcus aureus". Biochemistry. 38 (51): 16857–65. doi:10.1021/bi9911841. PMID 10606519.
    • Radabaugh TR, Aposhian HV (2000). "Enzymatic reduction of arsenic compounds in mammalian systems: reduction of arsenate to arsenite by human liver arsenate reductase". Chem. Res. Toxicol. 13 (1): 26–30. doi:10.1021/tx990115k. PMID 10649963.
    • Sato T, Kobayashi Y (1998). "The ars operon in the skin element of Bacillus subtilis confers resistance to arsenate and arsenite". J. Bacteriol. 180 (7): 1655–61. PMC 107075. PMID 9537360.
    • Shi J, Vlamis-Gardikas A, Aslund F, Holmgren A, Rosen BP (1999). "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 (51): 36039–42. doi:10.1074/jbc.274.51.36039. PMID 10593884.
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