Exceptionally versatile take II: post-translational modifications of lysine and their impact on bacterial physiology

Biol Chem. 2022 Feb 17;403(8-9):819-858. doi: 10.1515/hsz-2021-0382. Print 2022 Jul 26.

Abstract

Among the 22 proteinogenic amino acids, lysine sticks out due to its unparalleled chemical diversity of post-translational modifications. This results in a wide range of possibilities to influence protein function and hence modulate cellular physiology. Concomitantly, lysine derivatives form a metabolic reservoir that can confer selective advantages to those organisms that can utilize it. In this review, we provide examples of selected lysine modifications and describe their role in bacterial physiology.

Keywords: EF-P modifications; acylation; glycation; methylation; oxidation; pupylation.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / metabolism
  • Bacterial Physiological Phenomena
  • Lysine* / metabolism
  • Protein Processing, Post-Translational*
  • Proteins / metabolism

Substances

  • Amino Acids
  • Proteins
  • Lysine