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. 2012 May 30;287(30):25381–25394. doi: 10.1074/jbc.M112.372151

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© 2012 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 7. — Kinetic partitioning of aminoacyl-adenylate and aminoacylated tRNA within the synthetic (blue) and editing (red) sites, respectively. First-order rate constants for aminoacyl transfer and aa-tRNA deacylation were determined by single-turnover kinetics. Aminoacyl-adenylate hydrolysis and aa-tRNA dissociation are represented by steady-state rate constants (marked with an asterisk) that impose lower limits on the true values of the first-order microscopic rate constants for these steps. Dynamics of the cognate aa-tRNA translocation has not yet been investigated.