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. 2019 Nov;25(11):1481–1496. doi: 10.1261/rna.066746.118

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© 2019 Jaroensuk et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society

This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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FIGURE 6. — Analysis of steady-state kinetics of PaTrmD reveals a ternary complex mechanism. The in vitro PaTrmD assay was used to determine initial velocity (v_i) as a function of SAM and tRNA concentrations. The data were then subjected to a double-reciprocal plot for v_i determined at SAM concentrations ranging over 1–20 µM with different concentrations of tRNA^Leu(GAG): 0.4 µM (), 0.8 µM (), 1.6 µM (), 3.2 µM (), or 5 µM (). Data points represent mean ± SD for n = 3. The intersecting lines suggest that a ternary complex is required for the enzymatic reaction.

Inline graphic — Analysis of steady-state kinetics of PaTrmD reveals a ternary complex mechanism. The in vitro PaTrmD assay was used to determine initial velocity (v_i) as a function of SAM and tRNA concentrations. The data were then subjected to a double-reciprocal plot for v_i determined at SAM concentrations ranging over 1–20 µM with different concentrations of tRNA^Leu(GAG): 0.4 µM (), 0.8 µM (), 1.6 µM (), 3.2 µM (), or 5 µM (). Data points represent mean ± SD for n = 3. The intersecting lines suggest that a ternary complex is required for the enzymatic reaction.