Add time:08/19/2019         Source:sciencedirect.com

Arginyl-tRNA synthetase has a reaction mechanism not typical of most aminoacyl-tRNA synthetases. It does not catalyze an amino acid-dependent ATP-PP1 exchange in the absence of tRNA as do most enzymes of this class. In order to clarify the reaction mechanism by performing experiments with substrate levels of enzyme, we have modified the previous purification procedure. By the method presented, homogeneous enzyme can be prepared in approximately 10% yield. Pulse-labeling experiments indicate that no enzyme-bound arginyl-adenylate is formed in the absence of tRNA. Equilibrium experiments show that no arginyl-adenylate accumulates either in the presence or absence of tRNAarg. Two mechanisms compatible with these data are suggested.

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