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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
Aug 1, 2013 · Abstract. Selenium is an essential trace element that is incorporated into 25 human proteins as the amino acid selenocysteine (Sec). The incorporation of this amino acid turns out to be a fascinating problem in molecular biology because Sec is encoded by a stop codon, UGA. Layered on top of the canonical translation elongation machinery is a ...
- Jonathan N. Gonzalez-Flores, Sumangala P. Shetty, Aditi Dubey, Paul R. Copeland
- 10.1515/bmc-2013-0007
- 2013
- 2013/08/08
People also ask
How is selenocysteine encoded?
How selenocysteine is encoded in selenoprotein mRNA?
How is selenocysteine inserted into a nascent protein?
How is selenocysteine synthesized and incorporated into a selenoprotein?
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 ].
This page titled 6.1: Serine proteases is shared under a CC BY-NC-SA 4.0 license and was authored, remixed, and/or curated by Kevin Ahern & Indira Rajagopal. The serine proteases are a family of enzymes that cut certain peptide bonds in other proteins. This activity depends on a set of amino acid residues in the active site of the enzyme ...
Nov 25, 2021 · Only E. coli has a clear translation mechanism which contains a cis-acting element (Selenocysteine insertion sequence, SECIS) and four gene products , including SelA (selenocysteine synthetase, SecS), SelB (selenocysteine-specific elongation factor), SelC (tRNA [Ser]Sec) and SelD (seleno-phosphate
- 10.3390/molecules26237120
- 2021/12
- Molecules. 2021 Dec; 26(23): 7120.
May 15, 2022 · The serine proteases are a family of enzymes that cut certain peptide bonds in other proteins. This activity depends on a set of amino acid residues in the active site of the enzyme — one of which is always a serine (thus accounting for their name). In mammals, serine proteases perform many important functions, especially in digestion, blood ...
Oct 8, 2019 · In the deacylation step, a water molecule is activated by the histidine residue (general base catalysis) and it displaces the enzyme, via another tetrahedral intermediate. The departure of the protein serine is facilitated by the protonated histidine (general acid catalysis), returning the enzyme back to its original configuration.
