Selenocysteine: Difference between revisions
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Selenocysteine is called the 21st [[Amino Acids|amino acid]]<ref name='21st'>PMID: 11028985</ref>. | Selenocysteine (Sec) is called the 21st [[Amino Acids|amino acid]]<ref name='21st'>PMID: 11028985</ref>. It is incorporated into rare proteins in all domains of life, and is essential for life. When the UGA stop codon is accompanied by a [[#Translation from UGA Stop Codon|suitable signal]], it is translated as Sec instead of stopping translation. | ||
==Importance== | ==Importance== | ||
==Translation from UGA Stop Codon== | ==Translation from UGA Stop Codon== | ||
==Structure and Synthesis== | ==Structure and Synthesis== | ||
Cysteine (Cys) has a sulfur-containing side chain '''-CH<sub>2</sub>-SH''. In selenocysteine, the sulfur is replaced with selenium, making the side chain''' -CH<sub>2</sub>-SeH'''. | |||
Sec differs from the [[Amino Acids|20 standard amino acids]] because, in all domains of life, it lacks its own tRNA synthetase, and is synthesized from Ser covalently linked to tRNA<sup>Sec</sup>. | |||
==Notes and References== | ==Notes and References== | ||
<references /> | <references /> | ||
Revision as of 00:22, 27 July 2009
Selenocysteine (Sec) is called the 21st amino acid[1]. It is incorporated into rare proteins in all domains of life, and is essential for life. When the UGA stop codon is accompanied by a suitable signal, it is translated as Sec instead of stopping translation.
ImportanceImportance
Translation from UGA Stop CodonTranslation from UGA Stop Codon
Structure and SynthesisStructure and Synthesis
Cysteine (Cys) has a sulfur-containing side chain -CH2-SH. In selenocysteine, the sulfur is replaced with selenium, making the side chain' -CH2-SeH.
Sec differs from the 20 standard amino acids because, in all domains of life, it lacks its own tRNA synthetase, and is synthesized from Ser covalently linked to tRNASec.
Notes and ReferencesNotes and References
- ↑ Atkins JF, Gesteland RF. The twenty-first amino acid. Nature. 2000 Sep 28;407(6803):463, 465. PMID:11028985 doi:10.1038/35035189