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EcoSal Plus, 2004
About 50 years ago, research on the biological function of the element selenium was initiated by the report of J. Pinsent that generation of formate dehydrogenase activity by Escherichia coli requires the presence of both selenite and molybdate in the growth medium.
Böck, A. +1 more
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About 50 years ago, research on the biological function of the element selenium was initiated by the report of J. Pinsent that generation of formate dehydrogenase activity by Escherichia coli requires the presence of both selenite and molybdate in the growth medium.
Böck, A. +1 more
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International Journal of Biological Macromolecules, 2020 The selenocysteine (Sec) incorporation is a co-translational event taking place at an in-frame UGA-codon and dependent on an organized molecular machinery. Selenium delivery requires mainly two enzymes, the selenocysteine lyase (CsdB) is essential for Sec recycling and conversion to selenide, further used by the selenophosphate synthetase (SelD ...
Ana Paula Ulian de Araújo +2 more
exaly +4 more sources
EcoSal Plus, 2004
Selenocysteine is a naturally occurring analog of cysteine in which the sulfur atom of the latter is replaced with selenium. This seleno-amino acid occurs as a specific component of various selenoproteins and selenium-dependent enzymes.
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Selenocysteine is a naturally occurring analog of cysteine in which the sulfur atom of the latter is replaced with selenium. This seleno-amino acid occurs as a specific component of various selenoproteins and selenium-dependent enzymes.
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Selenium and Selenocysteine in Protein Chemistry
Angewandte Chemie - International Edition, 2017AbstractSelenocysteine, the selenium‐containing analogue of cysteine, is the twenty‐first proteinogenic amino acid. Since its discovery almost fifty years ago, it has been exploited in unnatural systems even more often than in natural systems. Selenocysteine chemistry has attracted the attention of many chemists in the field of chemical biology owing ...
Norman Metanis, Reem Mousa
exaly +3 more sources
Selenocysteine Biosynthesis and the Replacement of Selenocysteine with Cysteine in the Pathway
2011The biosynthetic pathway of selenocysteine (Sec), the 21st amino acid in the genetic code, has been established in eukaryotes and archaea using comparative genomic and experimental approaches. In addition, cysteine (Cys) was found to arise in place of selenocysteine in thioredoxin reductase (TR) in NIH 3T3 cells and in mice.
Xue-Ming Xu +5 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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Selenocysteine Metabolism in Mammals
1985Publisher 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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Catalysis of Electron Transfer by Selenocysteine
Biochemistry, 2006Selenium is an essential element that is involved in biological redox processes. The electrode potentials of the selenocysteine half-reactions RSe(*) + e(-) --> RSe-, (RSeSeR)(*)(-) + e(-) --> 2 RSe(-), and RSeSeR + 2 e(-) --> 2 RSe(-) [E degrees' (pH 7)] are +0.43, +0.18, and -0.38 V, respectively, at pH 7. The spectra of RSe(*) and (RSeSeR)(*)(-) are
Nauser T +3 more
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Analysis of Selenocysteine‐Containing Proteins
Current Protocols in Protein Science, 2000AbstractRepresentatives 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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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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