1245200-27-4Relevant academic research and scientific papers
Decoding the logic of the tRNA regiospecificity of nonribosomal femX Wv aminoacyl transferase www.angewandte.org
Fonvielle, Matthieu,Chemama, Maryline,Lecerf, Maxime,Villet, Regis,Busca, Patricia,Bouhss, Ahmed,Etheve-Quelquejeu, Melanie,Arthur, Michel
, p. 5115 - 5119 (2010)
Natural selection: Replacement of the 3′-OH group of Ala-tRNA Ala with 3′-H affected FemXWv-catalyzed aminoacyl transfer from the 2 -position, but not substrate binding. The ability of FemXWv to bind and transacylate the 3′-O-Ala isomer initially formed by alanyl-tRNA synthetase (AlaRS) may be crucial for efficient competition with the ribosome (see scheme). (Figure Presented).
