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  1. www.ncbi.nlm.nih.gov › pmc › articlesSynthesis and decoding of selenocysteine and human health

    Oct 9, 2012 · In all selenocysteine-containing organisms, the synthetic cycle of selenocysteine begins with an essential “error:” seryl-tRNA synthetase (SerRS) “erroneously” charges selenocysteine tRNA (tRNA Sec) with serine thus yielding seryl-tRNA Sec (Figure 1).

    • Figure 4

      Additionally, point mutations in the decoding apparatus...

    • Table 1

      Mutations linked to multiple muscle system disorders...

    • Open in a Separate Window

      Point mutations in SepSecS give rise to progressive...

  2. www.ncbi.nlm.nih.gov › pmc › articlesSelenoproteins: Molecular Pathways and Physiological Roles

    Research on the physiological roles and health benefits of Se has made tremendous progress following the discoveries that the amino acid residue in proteins, selenocysteine (Sec), is a major form of Se in the cell and that Sec is encoded by the UGA codon.

  3. www.ncbi.nlm.nih.gov › pmc › articlesThe Molecular Biology of Selenocysteine - PMC

    Aug 1, 2013 · The existence of a selenium-laden tRNA was first observed in experiments performed in rat liver where radiolabeled [75 Se]-selenite was associated with a tRNA-bound selenocysteine residue . In a follow-up article, Hawkes and Tappel showed that GPX incorporated [ 75 Se]-Sec when [ 75 Se]-Sec-tRNA was added in cell-free extracts from rat liver ...

    • Jonathan N. Gonzalez-Flores, Sumangala P. Shetty, Aditi Dubey, Paul R. Copeland
    • 10.1515/bmc-2013-0007
    • 2013
    • 2013/08/08

  4. link.springer.com › content › pdfMechanism, Structure, and Biological Role of Selenocysteine ...

    Selenite is then reduced to selenide by glutathione or thioredoxin reductase. 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 ].

  5. en.wikipedia.org › wiki › SelenocysteineSelenocysteine - Wikipedia

    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.

  6. chem.libretexts.org › Courses › University_of6.1: Serine proteases - Chemistry LibreTexts

    Found in our digestive system, chymotrypsin’s catalytic action is cleaving peptide bonds in proteins and it uses the side chain of a serine in its mechanism of catalysis. Many other protein- cutting enzymes employ a very similar mechanism and they are known collectively as serine proteases.

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  8. link.springer.com › article › 10Serine proteases: how did chemists tease out their catalytic ...

    Oct 8, 2019 · The first three display a hydroxyl (in serine and threonine proteases) or a thiol (in cysteine proteases) as the nucleophile in the protein, whereas the last three activate a water molecule from the media to act as the nucleophile (more on the mechanism below). Table 1 Types of proteases according to their catalytic type. Full size table.