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Selenocysteine Derivatives for Chemoselective Ligations
ChemBioChem, 2002AbstractFor Abstract see ChemInform Abstract in Full Text.
Matt D, Gieselman +4 more
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Bacterial selenocysteine synthase
European Journal of Biochemistry, 1998Selenocysteine synthase from Escherichia coli is a pyridoxal‐5′‐phosphate‐containing enzyme which catalyses the conversion of seryl‐tRNASec into selenocysteyl‐tRNASec. Analysis of amino acid sequences indicated that selenocysteine synthase belongs to the α/γ superfamily of pyridoxal‐5′‐phosphate‐dependent enzymes.
P, Tormay +5 more
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2001
The selenocysteine (Sec) tRNA population in mammals consists of two major isoforms that differ from each other by a single methylation group on the 2’-O-ribosyl moiety at position 34. The tRNAs are 90 nucleotides in length making them the longest eukaryotic tRNAs sequenced to date. Both tRNAs decode UGA and arise from a single copy gene.
Bradley A. Carlson +6 more
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The selenocysteine (Sec) tRNA population in mammals consists of two major isoforms that differ from each other by a single methylation group on the 2’-O-ribosyl moiety at position 34. The tRNAs are 90 nucleotides in length making them the longest eukaryotic tRNAs sequenced to date. Both tRNAs decode UGA and arise from a single copy gene.
Bradley A. Carlson +6 more
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Selenocysteine and selenoproteins
2004Selenium occurs normally in living things as a highly specific component of certain enzymes and amino acid transfer nucleic acids (tRNAs). In bacteria, biosynthesis of essential selenoenzymes has been shown to be unaffected by wide variations in sulfur levels.
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RNA binding proteins and selenocysteine
BioFactors, 2001AbstractSelenocysteine is incorporated into protein by a complex co‐translational mechanism that involves both cis and trans acting factors. Among the trans‐acting factors are RNA binding proteins that interact with the selenoprotein 3′ UTRs at a sequence known as the selenocysteine insertion sequence (SECIS). These factors are generally referred to as
P R, Copeland, D M, Driscoll
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Biotechnology of selenocysteine
2007In this chapter we describe strategies to produce synthetic selenoproteins, with a focus on recombinant selenoprotein production in E. coll. We further discuss the possible use of selenocysteine (Sec) in proteins for biotechnological applications.
Linda Johansson, Elias S. J. Arnér
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Selenocystein β-lyase (porcine)
1987Publisher Summary Selenocysteine β -1yase catalyzes specifically the β-elimination reaction of L-selenocysteine to form L-alanine and elemental selenium. The enzyme occurs widely in various mammalian tissues and in the cells of aerobic bacteria. The enzyme has been purified to homogeneity from pig liver and from Citrobacter freundii.
Nobuyoshi Esaki, Kenji Soda
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