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- Rather, the tRNA-bound seryl residue is converted to a selenocysteine residue by the pyridoxal phosphate -containing enzyme selenocysteine synthase. 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.
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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.
- Table 1
Mutations linked to multiple muscle system disorders...
- 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
Baron C, Böck A (1991) The length of the aminoacyl-acceptor...
- Structure of a tRNA-dependent Kinase Essential for Selenocysteine Decoding
Overall Structure. The crystal structure of MjPSTK was...
- Table 1
Rather, the tRNA-bound seryl residue is converted to a selenocysteine residue by the pyridoxal phosphate-containing enzyme selenocysteine synthase. 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.
- C₃H₇NO₂Se
- .mw-parser-output .plainlist ol,.mw-parser-output .plainlist ul{line-height:inherit;list-style:none;margin:0;padding:0}.mw-parser-output .plainlist ol li,.mw-parser-output .plainlist ul li{margin-bottom:0}10236-58-5
- 168.065 g·mol−1
- CHEBI:16633
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 , which is produced from selenide and ATP by selenophosphate synthetase [ 5 , 6 ].
Aug 1, 2013 · By 1976 the research group of Thressa C. Stadtman had discovered that selenium was covalently attached in the C. sticklandii glycine reductase as a selenocysteine residue ( 10 ). This finding was also confirmed in GPX where the catalytic site was identified as selenocysteine ( 11 ).
- Jonathan N. Gonzalez-Flores, Sumangala P. Shetty, Aditi Dubey, Paul R. Copeland
- 10.1515/bmc-2013-0007
- 2013
- 2013/08/08
Jan 22, 2020 · The initial Ser residue present in the Ser-tRNA [Ser]Sec is phosphorylated by PSTK, resulting in an intermediate o-phosposeryl- (Sep)-tRNA [Sep]Sec. Following the conversion, the o-phosphoseryl-tRNA Sec selenium transferase (SepSecS–a PLP-dependent enzyme) performs the Sep/Sec conversion, resulting in the mature Sec-tRNA Sec ( Liu et al., 2014 ).
- Vitor Hugo Balasco Serrão, Jessica Fernandes Scortecci
- 2020
Nov 15, 2022 · Highlights. •. Organized outline of tools used for studying selenocysteine. •. Detailed bacterial and eukaryotic systems used for selenoprotein production. •. Collection of probes to detect selenocysteine in vitro and in vivo. •. Databases and programs to find selenoproteins in genomic databases. Abstract.
The role of selenium is mainly played through selenoproteins synthesized by the selenium metabolic system. Selenoproteins have a wide range of cellular functions including regulation of selenium...
