Results 171 to 180 of about 20,702 (201)

Analysis of Selenocysteine‐Containing Proteins

Current Protocols in Protein Science, 2000
AbstractRepresentatives of three primary life domains‐‐bacteria, archaea, and eukaryotes‐‐possess specific selenium‐containing proteins. The majority of naturally occurring selenoproteins contain an amino acid, selenocysteine, that is incorporated into protein in response to the code word UGA.
V N, Gladyshev, D L, Hatfield
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Selenocysteine Metabolism in Mammals

1985
Publisher Summary This chapter discusses selenocysteine metabolism in mammals. Several microbial and mammalian proteins, particularly enzymes, contain selenium as an essential component. Four of them have been shown to contain a selenocysteine residue in their polypeptide chains: selenoprotein A of glycine reductase complex from Clostridium ...
H, Tanaka, N, Esaki, K, Soda
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Se-ing into selenocysteine biosynthesis

Nature Chemical Biology, 2009
A cocrystal structure of the enzyme that synthesizes selenocysteine reveals the elegantly simple recognition mechanism for the tRNA molecule for this '21st amino acid'. The structure resolves some mechanistic questions and allows for comparison of the tRNA-dependent synthesis of cysteine and selenocysteine.
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Selenocysteine Derivatives for Chemoselective Ligations

ChemBioChem, 2002
AbstractFor Abstract see ChemInform Abstract in Full Text.
Matt D, Gieselman, Yantao, Zhu, Hao, Zhou, Danica, Galonic, Wilfred A, van der Donk   +4 more
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Bacterial selenocysteine synthase

European Journal of Biochemistry, 1998
Selenocysteine 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, R, Wilting, F, Lottspeich, P K, Mehta, P, Christen, A, Böck   +5 more
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Mammalian selenocysteine tRNA

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, F. Javier Martin-Romero, Easwari Kumaraswamy, Mohamed E. Moustafa, Huijun Zhi, Dolph L. Hatfield, Byeong Jae Lee   +6 more
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Selenocysteine and selenoproteins

2004
Selenium 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, 2001
AbstractSelenocysteine 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

2007
In 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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Selenocysteine

1987
H, Tanaka, K, Soda
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