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Oct 9, 2012 · Emerging evidence suggests that enzymes responsible for selenocysteine formation and decoding the selenocysteine UGA codon, which by extension are critical for synthesis of the entire selenoproteome, are essential for the development and health of the human organism.
- Figure 4
The essentiality of the selenocysteine cycle has also been...
- Table 1
GpX1-4, GpX6. Glutathione peroxidase. Catalyzes the...
- Open in a Separate Window
Point mutations in SepSecS give rise to progressive...
- The Selenocysteine-specific Elongation Factor Contains a Novel and Multi-functional Domain
The selenocysteine (Sec)-specific eukaryotic elongation...
- Secis
Background: Selenocysteine incorporation requires unique...
- PMC Free Article
Ser-tRNA Sec recognition was tested by transferring SelB...
- Structure of a tRNA-dependent Kinase Essential for Selenocysteine Decoding
Overall Structure. The crystal structure of MjPSTK was...
- Figure 4
Oct 30, 2005 · All of the methods are based on either the introduction of a selenium isotope, with specific characteristics such as high-energy radioactivity (as for 75 Se and 73 Se) or uncommon nuclear spin ( 77 Se), or on the high reactivity of a Sec residue in comparison to Cys. Table 5.
- Linda Johansson, Guro Gafvelin, Elias S.J. Arnér
- 2005
In eukaryotes and archaea, two enzymes are required to convert tRNA-bound seryl residue into tRNA selenocysteinyl residue: PSTK (O-phosphoseryl-tRNA[Ser]Sec kinase) and selenocysteine synthase.
Although selenoproteins represent diverse molecular pathways and biological functions, all these proteins contain at least one selenocysteine (Sec), a selenium-containing amino acid, and most serve oxidoreductase functions.
Aug 1, 2013 · Interestingly, a single Sec residue resides in the N-terminus while the remaining are primarily located in the C-terminus . The N-terminus of SelP has been shown to have potential weak antioxidant role while the C-terminus is essential for selenium distribution (65,131).
- Jonathan N. Gonzalez-Flores, Sumangala P. Shetty, Aditi Dubey, Paul R. Copeland
- 10.1515/bmc-2013-0007
- 2013
- 2013/08/08
Our approach makes use of “native chemical ligation.” 8,9 Native chemical ligation allows for two peptide chains to be joined chemoselectively through the use of a C-terminal thioester on one peptide and an N-terminal cysteine residue on the other peptide ( Fig. 1 ).
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How is selenocysteine encoded?
How is selenocysteine synthesized and incorporated into a selenoprotein?
What reveals the mechanism of selenocysteine formation?
As shown in Fig. 10.1 , selenide is the key compound for selenoprotein biosyn-thesis . A selenocysteine residue is encoded by the UGA codon in selenoprotein mRNA , which is decoded by selenocysteyl-tRNA [Ser]Sec [ 3 , 4 ]. The selenocysteine moiety on selenocysteyl-tRNA [Ser]Sec is biosynthesized using selenophosphate ,