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March 18, 2026Journal of the American Chemical SocietyOpen Access

Expanding the Genetic Code with Lysine Aminoacylation

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Authors

XLXinyu LiQGQinglei GanCFChenguang Fan

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Overview

Finds effects of lysine aminoacylation on metabolic enzymes in human cells, suggesting new research tools for protein modification.

Key Points

  • To explore the function of lysine aminoacylation and develop methods to produce homogeneously modified proteins.
  • Engineered pyrrolysyl-tRNA synthetase for lysine aminoacylation
  • Established orthogonal translation systems in bacterial and mammalian cells
  • Tested effects of lysine aminoacylation on metabolic enzymes
  • Lysine valylation impaired the activity of pyruvate kinase
  • Lysine tyrosylation impaired glucose-6-phosphate dehydrogenase activity
  • Lysine valylation of pyruvate kinase decreased basal glycolytic rate in living human cells

Cite This Study

Li et al. (2026) studied this question.

synapsesocial.com/papers/69ba429c4e9516ffd37a2ff3https://doi.org/10.1021/jacs.6c03157
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1A Modular Genetic Code Expansion Approach to Site-Specific Lysine Acylations2025
  2. 2Non-hydrolyzable acetyllysine analogs to study protein acetylation in vitro and in cells2026
  3. 3Genetic code expansion reveals site-specific lactylation in living cells reshapes protein function2024 · 2 citations
  4. 4Precision Chemistry and Activity-Based Proteomics for Posttranslational Control of Protein Function2024
  5. 5Deciphering functional roles of protein succinylation and glutarylation using genetic code expansion2024 · 47 citations