Study on the putative active site of Enterococcus faecalisprolyl- tRNA synthetase editing domain by methods of site-directed mutagenesis

Study on the putative active site of Enterococcus faecalisprolyl- tRNA synthetase editing domain by methods of site-directed mutagenesis

The maintenance of amino acid specificity by aminoacyl-tRNA synthetases can require the hydrolysis of missynthesized products that is known as amino acid editing. Bacterial prolyl-tRNA synthetase includes a special editing domain, that deacylates alanyl-tRNA

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Bibliographische Detailangaben
Veröffentlicht in:Biopolimery i kletka 2009-01, Vol.25 (1), p.39
Hauptverfasser: Boyarshin, K S, Kriklivyi, I A, Rayevsky, A V, Himin, A A, Yaremchuk, A D, Tukalo M. A.
Format: Artikel
Sprache:eng
Schlagworte:
Amino acids
Editing
Proline-tRNA ligase
Site-directed mutagenesis
tRNA
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Beschreibung
Zusammenfassung:The maintenance of amino acid specificity by aminoacyl-tRNA synthetases can require the hydrolysis of missynthesized products that is known as amino acid editing. Bacterial prolyl-tRNA synthetase includes a special editing domain, that deacylates alanyl-tRNA
ISSN:0233-7657
1993-6842
DOI:10.7124/bc.0007C8