The Enzyme Database

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EC 1.20.4.1     
Accepted name: arsenate reductase (glutaredoxin)
Reaction: arsenate + glutaredoxin = arsenite + glutaredoxin disulfide + H2O
For diagram of arsenate catabolism, click here
Systematic name: glutharedoxin:arsenate oxidoreductase
Comments: A molybdoenzyme. The glutaredoxins catalyse glutathione-disulfide oxidoreductions and have a redox-active disulfide/dithiol in the active site (-Cys-Pro-Tyr-Cys-) that forms a disulfide bond in the oxidized form [2, 10]. Glutaredoxins have a binding site for glutathione, which is required to reduce them to the dithiol form [3,6]. Thioredoxins reduced by NADPH and thioredoxin reductase can act as alternative substrates. The enzyme [1, 4, 7, 9] 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 to non-toxic organoarsenical compounds.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 146907-46-2
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 (1996) 33256–33260. [PMID: 8969183]
2.  Gladysheva, T.B., Oden, K.L. and Rosen, B.P. Properties of the arsenate reductase of plasmid R773. Biochemistry 33 (1994) 7288–7293. [PMID: 8003492]
3.  Holmgren, A. and Aslund, F. Glutaredoxin. Methods Enzymol. 252 (1995) 283–292. [PMID: 7476363]
4.  Ji, G.Y., Garber, E.A.E., Armes, L.G., Chen, C.M., Fuchs, J.A. and Silver, S. Arsenate reductase of Staphylococcus aureus plasmid PI258. Biochemistry 33 (1994) 7294–7299.
5.  Krafft, T. and Macy, J.M. Purification and characterization of the respiratory arsenate reductase of Chrysiogenes arsenatis. Eur. J. Biochem. 255 (1998) 647–653. [PMID: 9738904]
6.  Martin, J.L. Thioredoxin - a fold for all reasons. Structure 3 (1995) 245–250. [PMID: 7788290]
7.  Messens, J., Hayburn, G., Desmyter, A., Laus, G. and Wyns, L. The essential catalytic redox couple in arsenate reductase from Staphylococcus aureus. Biochemistry 38 (1999) 16857–16865. [PMID: 10606519]
8.  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 (2000) 26–30. [PMID: 10649963]
9.  Sato, T. and Kobayashi, Y. The ars operon in the skin element of Bacillus subtilis confers resistance to arsenate and arsenite. J. Bacteriol. 180 (1998) 1655–1661. [PMID: 9537360]
10.  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 (1999) 36039–36042. [PMID: 10593884]
[EC 1.20.4.1 created 2000 as EC 1.97.1.5, transferred 2001 to EC 1.20.4.1]
 
 


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