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. 2023 Mar 23;51(7):3327–3340. doi: 10.1093/nar/gkad205

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© The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (https://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 5. — Chiral selectivity of AlaRS aminoacylation site. (A) Deacylation of L-Ala-tRNA^Ala by both EcDTD and EcAlaRS-WT. (B) Deacylation of D-Ala-tRNA^Ala (AlaRS generated aminoacylated substrate) by EcAlaRS-WT and EcDTD showing that D-Ala-tRNA^Ala is not cleaved by either of them. (C) Deacylation of L-Ala-tRNA^Ala charged by flexizyme by EcAlaRS-WT and EcDTD showing similar results as AlaRS charged substrate. (D) Deacylation of flexizyme charged D-Ala-tRNA^Ala by EcAlaRS-WT and EcDTD shows that EcDTD can effectively cleave D-Ala-tRNA^Ala but not by EcAlaRS-WT. (E) Aminoacylation of L-Ala and D-Ala on tRNA^Ala by EcAlaRS C666A with reducing concentration of the amino acid substrate in the reaction (100 mM, 10 mM, 1 mM, 100 μM, 10 μM, 1 μM and 100 nM) showing L-alanine getting charged at 10 μM amino acid concentration, which is 1000-fold less than the minimum concentration at which D-alanine charging is seen, i.e. 10 mM.