The Enzyme Database

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EC 1.97.1.9     
Accepted name: selenate reductase
Reaction: selenite + H2O + acceptor = selenate + reduced acceptor
Systematic name: selenite:reduced acceptor oxidoreductase
Comments: The periplasmic enzyme from Thauera selenatis is a complex comprising three heterologous subunits (α, β and γ) that contains molybdenum, iron, acid-labile sulfide and heme b as cofactor constituents. Nitrate, nitrite, chlorate and sulfate are not substrates. A number of compounds, including acetate, lactate, pyruvate, and certain sugars, amino acids, fatty acids, di- and tricarboxylic acids, and benzoate can serve as electron donors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 146359-71-9
References:
1.  Schröder, I., Rech, S., Krafft, T. and Macy, J.M. Purification and characterization of the selenate reductase from Thauera selenatis. J. Biol. Chem. 272 (1997) 23765–23768. [PMID: 9295321]
2.  Macy, J.M., Rech, S., Auling, G., Dorsch, M., Stackebrandt, E. and Sly, L.I. Thauera selenatis gen. nov., sp. nov., a member of the β subclass of Proteobacteria with a novel type of anaerobic respiration. Int. J. Syst. Bacteriol. 43 (1993) 135–142. [PMID: 8427805]
3.  Krafft, T., Bowen, A., Theis, F. and Macy, J.M. Cloning and sequencing of the genes encoding the periplasmic-cytochrome B-containing selenate reductase of Thauera selenatis. DNA 10 (2000) 365–377. [PMID: 10826693]
4.  Stolz, J.F. and Oremland, R.S. Bacterial respiration of arsenic and selenium. FEMS Microbiol. Rev. 23 (1999) 615–627. [PMID: 10525169]
[EC 1.97.1.9 created 2003]
 
 


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