Abstract
Selenium occurs normally in living things as a highly specific component of certain enzymes and amino acid transfer nucleic acids (tRNAs). In bacteria, biosynthesis of essential selenoenzymes has been shown to be unaffected by wide variations in sulfur levels. The naturally occurring selenoenzymes identified from bacterial sources include glycine reductase, formate dehydrogenases, a hydrogenase, nicotinic acid hydroxylase, xanthine dehydrogenase. The selenoenzyme, glutathione peroxidase, and other selenoproteins of unknown function have been isolated from animals. In certain enzymes, e.g. glycine reductase, formate dehydrogenase, hydrogenase and glutathione peroxidase, the chemical form of selenium has been identified as selenocysteine. A labile, unidentified form of selenium is present in nicotinic acid hydroxylase, and by inference, xanthine dehydrogenase.
Keywords
Electron Paramagnetic Resonance Electron Paramagnetic Resonance Signal Formate Dehydrogenase Xanthine Dehydrogenase Selenoprotein GeneSelected References
- Böck A (2001) Selenium metabolism in bacteria. In: Hatfield DL (ed) Selenium: its molecular biology and role in human health. Kluwer Academic, Dordrecht, pp 7–22CrossRefGoogle Scholar
- Low SC, Grundner-Culemann E, Harney JW, Berry MJ (2000) EMBO J 19:6882–6890PubMedCentralPubMedCrossRefGoogle Scholar
- Lu J, Holmgren A (2009) J Biol Chem 284:723–727PubMedCrossRefGoogle Scholar
- Schumann S, Saggu M, Moller N, Anker SD, Lendzian F, Hildebrandt P, Leimkuhler S (2008) J Biol Chem 283:16602–16611PubMedCrossRefGoogle Scholar
- Stadtman TC (1996) Ann Rev Biochem 65:83–100PubMedCrossRefGoogle Scholar
- Stadtman TC (2002) J Biol Chem 277:49091–49100PubMedCrossRefGoogle Scholar
- Suzuki M, Lee D-Y, Inyamah N, Stadtman TC, Tjandra N (2008) J Biol Chem 283:25936–25943PubMedCentralPubMedCrossRefGoogle Scholar
- Thanbichler M, Böck A (2002) EMBO J 24:6925–6934CrossRefGoogle Scholar