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Selenium Is Mobilized In Vivo from Free Selenocysteine and Is Incorporated Specifically into Formate Dehydrogenase H and tRNA Nucleosides. Gerard M. Lacourciere, 2002.Selenophosphate synthetase (SPS), the selD gene product from Escherichia coli, catalyzes the biosynthesis of monoselenophosphate, AMP, and orthophosphate in a 1:1:1 ratio from selenide and ATP . It was recently demonstrated that selenium delivered from selenocysteine by an E . coli NifS-like protein could replace free selenide in the in vitro SPS assay for selenophosphate formation (G . M . Lacourciere, H . Mihara, T . Kurihara, N . Esaki, and T . C . Stadtman, J . Biol . Chem . 275:23769-23773, 2000) . During growth of E . coli in the presence of 0.1 µM 75SeO32- and increasing amounts of L-selenocysteine, a concomitant decrease in 75Se incorporation into formate dehydrogenase H and nucleosides of bulk tRNA was observed . This is consistent with the mobilization of selenium from L-selenocysteine in vivo and its use in selenophosphate formation . The ability of E . coli to utilize selenocysteine as a selenium source for selenophosphate biosynthesis in vivo supports the participation of the NifS-like proteins in selenium metabolism .
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