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PMID: 1838215 Published · ppublish English Journal Article Review

Selenoprotein synthesis: an expansion of the genetic code.

Trends in biochemical sciences ·Vol. 16 ·No. 12 ·1991-12-00 ·Pages 463-7

Böck A, Forchhammer K, Heider J, Baron C

Abstract

A number of enzymes employ the unusual amino acid selenocysteine as part of their active site because of its high chemical reactivity. Selenocysteine is incorporated into these proteins co-translationally: biosynthesis occurs on a specific tRNA and insertion into a growing polypeptide is directed by a UGA codon in the mRNA. In E. coli, this requires a specific translation factor. Selenocysteine thus represents a unique expansion of the genetic code.

MeSH Terms
Animals Base Sequence Codon Cysteine/analogs & derivatives,biosynthesis,genetics Escherichia coli/genetics Genetic Code Humans Molecular Sequence Data Organoselenium Compounds Protein Biosynthesis Proteins/genetics RNA, Messenger/genetics RNA, Transfer, Amino Acid-Specific/genetics Selenium/metabolism Selenocysteine Selenoproteins
Chemicals
Codon Organoselenium Compounds Proteins RNA, Messenger RNA, Transfer, Amino Acid-Specific Selenoproteins Selenocysteine Selenium Cysteine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Böck A
Lehrstuhl für Mikrobiologie, Universität München, FRG.
Forchhammer K
Heider J
Baron C
Article Info
Journal
Trends in biochemical sciences
Abbr.
Trends Biochem Sci
ISSN
0968-0004
Published
1991-12-00
Pages
463-7
Language
English
Region
England
NLM ID
7610674
Subset
IM
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