Related Experiment Video
Updated: May 16, 2026

Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells
Published on: February 24, 2026
Lysine biosynthesis in bacteria: a metallodesuccinylase as a potential antimicrobial target
Danuta M Gillner1,2, Daniel P Becker3, Richard C Holz4
1Department of Chemistry and Biochemistry, Loyola University-Chicago, 1068 W. Sheridan Rd., Chicago, IL, 60626, USA. danuta.gilner@polsl.pl.
Abstract:
In this review, we summarize the recent literature on dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) enzymes, with an emphasis on structure-function studies that provide insight into the catalytic mechanism. Crystallographic data have also provided insight into residues that might be involved in substrate and hence inhibitor recognition and binding. These data have led to the design and synthesis of several new DapE inhibitors, which are described along with what is known about how inhibitors interact with the active site of DapE enzymes, including the efficacy of a moderately strong DapE inhibitor.
Related Concept Videos
Inhibitors of Bacterial Protein Synthesis
Gene Regulation in Microbial Communities: Quorum Sensing
Biosynthesis in Bacteria
Inhibitors of Gram-positive Cell Wall Synthesis
Biological Methods for Microbial Control
Clinical Significance of Antibiotic Resistance

