Arsenate reductase (glutaredoxin)

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.

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.

Other oxidoreductases (EC 1.15-1.21)

1.15: Acting on superoxide as acceptor	Superoxide dismutase SOD1 SOD2 SOD3

1.16: Oxidizing metal ions	Ceruloplasmin

1.17: Acting on CH or CH2 groups	Xanthine oxidase Ribonucleotide reductase 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase

1.18: Acting on iron-sulfur proteins as donors	Nitrogenase

1.19: Acting on reduced flavodoxin as donor	Nitrogenase (flavodoxin)

1.20: Acting on phosphorus or arsenic in donors	Glutaredoxin GLRX GLRX2 GLRX3 GLRX5

1.21: Acting on X-H and Y-H to form an X-Y bond	Isopenicillin N synthase

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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