ReviewFEBS letters2025
Mechanisms and kinetic assays of aminoacyl-tRNA synthetases.
Review in FEBS letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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3 authors.
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Abstract
Accurate protein synthesis is crucial for life. The key players are aminoacyl-tRNA synthetases (AARSs), which read the genetic code by pairing cognate amino acids and tRNAs. AARSs establish high amino acid selectivity by employing physicochemical limits in molecular recognition. However, chemical and structural resemblance between some amino acids prevents their efficient discrimination by AARSs. In these cases, AARSs hydrolyze the formed non-cognate intermediates or aa-tRNAs to ensure selectivity, establishing complex reaction pathways within the synthetic and editing sites. Understanding AARS mechanisms is crucial for understanding their biology. Here, we review kinetic assays for exploring AARS mechanisms. For each assay, we state the most suitable substrates, product(s) recommended to follow, and, importantly, possible caveats that may lead to the kinetic artefact.
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