On the mechanism of tRNATrp aminoacylation catalysed by beef tryptophanyl‐tRNA synthetase using presteady‐state kinetics

FEBS Letters

Labouesse, Bernard¹  Merle, Michel¹  Gandar, J.C.¹  Trezeguet, Véronique¹ 

[1] Institut de Biochimie Cellulaire et Neurochimie, CNRS, 1 rue Camille, St-Saëns, 33077 Bordeaux, France

关键词: tRNA;    Aminoacylation;    Aminoacyl-tRNA synthetase;    Presteady-state kinetics;   

DOI  :  10.1016/0014-5793(83)81147-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The dimeric tryptophanyl-tRNA synthetase from beef pancreas has been found to activate 2 tryptophans/mol enzyme [Eur. J. Biochem. (1982) 128, 389–398]. By using quenched-flow and stopped-flow methods under presteady-state conditions, we show that only one enzyme subunit operates at a time in the aminoacylation of tRNA^Trp and that the transfer reaction is not the rate-limiting step in the overall aminoacylation process.

【 授权许可】

Unknown