Results 131 to 140 of about 11,168 (173)

Selenocysteine Lyase

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 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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Selenocysteine Biosynthesis and the Replacement of Selenocysteine with Cysteine in the Pathway

2011
The 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, Anton A. Turanov, Bradley A. Carlson, Min-Hyuk Yoo, Vadim N. Gladyshev, Dolph L. Hatfield   +5 more
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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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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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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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Catalysis of Electron Transfer by Selenocysteine

Biochemistry, 2006
Selenium 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, Dockheer S, Kissner R, Koppenol WH   +3 more
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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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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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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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