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
Other name(s): ArsC (ambiguous)
Systematic name: arsenate:glutaredoxin oxidoreductase
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: 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.  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]
5.  Martin, J.L. Thioredoxin - a fold for all reasons. Structure 3 (1995) 245–250. [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 (2000) 26–30. [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 (1998) 1655–1661. [PMID: 9537360]
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 (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, modified 2015]
 
 


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