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Decoding the Logic of the tRNA Regiospecificity of Nonribosomal FemX Wv Aminoacyl Transferase
Author(s) -
Fonvielle Matthieu,
Chemama Maryline,
Lecerf Maxime,
Villet Régis,
Busca Patricia,
Bouhss Ahmed,
EthèveQuelquejeu Mélanie,
Arthur Michel
Publication year - 2010
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201001473
Subject(s) - transfer rna , transferase , chemistry , computer science , computational biology , stereochemistry , biology , biochemistry , enzyme , gene , rna
Natural selection : Replacement of the 3′‐OH group of Ala‐tRNA Ala with 3′‐H affected FemX Wv ‐catalyzed aminoacyl transfer from the 2′‐position, but not substrate binding. The ability of FemX Wv 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).