Selenate reductase | |||||||||
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Identifiers | |||||||||
EC no. | 1.97.1.9 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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In enzymology, a selenate reductase (EC 1.97.1.9) is an enzyme that catalyzes the chemical reaction
- selenite + H2O + acceptor selenate + reduced acceptor
The 3 substrates of this enzyme are selenite, H2O, and acceptor, whereas its two products are selenate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is selenite:reduced acceptor oxidoreductase.
References
- Schroder I, Rech S, Krafft T, Macy JM (1997). "Purification and characterization of the selenate reductase from Thauera selenatis". J. Biol. Chem. 272 (38): 23765–8. doi:10.1074/jbc.272.38.23765. PMID 9295321.
- Macy JM, Rech S, Auling G, Dorsch M, Stackebrandt E, Sly LI (1993). "Thauera selenatis gen. nov., sp. nov., a member of the beta subclass of Proteobacteria with a novel type of anaerobic respiration". Int. J. Syst. Bacteriol. 43 (1): 135–42. doi:10.1099/00207713-43-1-135. PMID 8427805.
- Krafft T, Bowen A, Theis F, Macy JM (2000). "Cloning and sequencing of the genes encoding the periplasmic-cytochrome B-containing selenate reductase of Thauera selenatis". DNA Seq. 10 (6): 365–77. doi:10.3109/10425170009015604. PMID 10826693.
- Stolz JF, Oremland RS (1999). "Bacterial respiration of arsenic and selenium". FEMS Microbiol. Rev. 23 (5): 615–27. doi:10.1111/j.1574-6976.1999.tb00416.x. PMID 10525169.
Other oxidoreductases (EC 1.15–1.21) | |
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1.15: Acting on superoxide as acceptor | |
1.16: Oxidizing metal ions | |
1.17: Acting on CH or CH2 groups | |
1.18: Acting on iron–sulfur proteins as donors | |
1.19: Acting on reduced flavodoxin as donor | |
1.20: Acting on phosphorus or arsenic in donors | |
1.21: Acting on X-H and Y-H to form an X-Y bond |
Enzymes | |
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Activity | |
Regulation | |
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