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Investigating Mycobacterium tuberculosis L,D‐transpeptidases as novel drug targets

The final step of peptidoglycan (PG) biosynthesis in bacteria involves cross‐linking of peptide side chains. This step in Mycobacterium tuberculosis is catalyzed by L,D‐ and D,D‐transpeptidases that generate 3→3 and 4→3 transpeptide linkages, respectively. M. tuberculosis PG is predominantly 3→3 cross‐linked, and LdtMt2 is the dominant L,D‐transpeptidase. There are four additional sequence paralogs of LdtMt2 encoded by the genome of this pathogen, and the reason for this apparent redundancy is unknown. Here, we present microbiological, biochemical, and structural data suggesting paralogs LdtMt2, LdtMt3, and LdtMt5 are not functionally redundant. Further, we demonstrate that at least two of these paralogs are acylated by carbapenem antibiotics. Importantly, the work presented here provides structural evidence of acylation of LdtMt2 by tebipenem, an orally available carbapenem, and biapenem.