Over 500 natural and synthetic amino acids have been genetically encoded in the last two
decades. Incorporating these noncanonical amino acids into proteins enables many …

Aminoacyl‐tRNA synthetases (AARSs) charge tRNA with their cognate amino acids. Many
other enzymes use amino acids as substrates, yet discrimination against noncognate amino …

Error-free translation of the genetic code into proteins is vitally important for all organisms.
Therefore, it is crucial that the correct amino acids are loaded onto their corresponding …

Aminoacyl-tRNA synthetases (AARS) translate the genetic code by loading tRNAs with the
cognate amino acids. The errors in amino acid recognition are cleared at the AARS editing …

Antibiotics target key biological processes that include protein synthesis. Bacteria respond
by developing resistance, which increases rapidly due to antibiotics overuse. Mupirocin, a …

Abstract Aminoacyl-tRNA synthetases (aaRSs), the enzymes responsible for coupling tRNAs
to their cognate amino acids, minimize translational errors by intrinsic hydrolytic editing …

Isoleucyl‐tRNA synthetase (IleRS) is an essential enzyme that covalently couples isoleucine
to the corresponding tRNA. Bacterial IleRSs group in two clades, ileS1 and ileS2, the latter …

The intrinsic editing capacities of aminoacyl-tRNA synthetases ensure a high-fidelity
translation of the amino acids that possess effective non-cognate aminoacylation surrogates …

Error-free translation of the genetic code into proteins is vitally important for all organisms.
Therefore, it is crucial that the correct amino acids are loaded onto their corresponding …

To correctly aminoacylate tRNALeu, leucyl-tRNA synthetase (LeuRS) catalyzes three
reactions: activation of leucine by ATP to form leucyl-adenylate (Leu-AMP), transfer of this …