Exceptionally versatile take II: Post-Translational modifications of lysine and their impact on bacterial physiology
Research output: Contribution to journal › Review article › Contributed › peer-review
Contributors
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.
Details
Original language | English |
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Pages (from-to) | 819-858 |
Number of pages | 40 |
Journal | Biological chemistry |
Volume | 403 |
Issue number | 8-9 |
Early online date | 17 Feb 2022 |
Publication status | Published - 26 Jul 2022 |
Peer-reviewed | Yes |
Externally published | Yes |
External IDs
PubMed | 35172419 |
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unpaywall | 10.1515/hsz-2021-0382 |
Mendeley | fa735682-e71c-34ae-b05d-28e0ae4060a2 |
ORCID | /0000-0001-8528-6893/work/142256519 |
Keywords
ASJC Scopus subject areas
Keywords
- acylation, EF-P modifications, glycation, methylation, oxidation, pupylation, Proteins/metabolism, Lysine/metabolism, Bacterial Physiological Phenomena, Protein Processing, Post-Translational, Amino Acids/metabolism