Abstract
There currently are 7 known bacterial selenoenzymes. All but thiolase contain selenocysteine (Se-Cys), presumably at the active site, and all but thiolase catalyze oxidation-reduction reactions. Selenide appears to be a central intermediate in selenium (Se) metabolism in animals, and it may be the precursor used for formation of the Se-Cys moiety in glutathione peroxidase (GSH-Px). The incorporation of Se into GSH-Px appears to occur via a post-translational mechanism, but the nature and extent of Se-Cys formation in higher animals has not been established. GSH-Px deficiency remains a logical explanation for a number of Se-deficiency signs, but other known selenoproteins and other functions may match up with defects apparently not prevented by GSH-Px.
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Sunde, R.A. The biochemistry of selenoproteins. J Am Oil Chem Soc 61, 1891–1900 (1984). https://doi.org/10.1007/BF02540827
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DOI: https://doi.org/10.1007/BF02540827