As antibiotic resistance continues to grow, uncovering new avenues for antimicrobial development is crucial. Over the past decade, the enzymes of lysine biosynthesis have emerged as promising antibacterial targets, being necessary for such essential processes as cell-wall and siderophore biosynthesis as well as the production of lysine itself. Two early steps in the pathway involve acylation of meso-diaminopimelate (meso-DAP) followed by PLP-dependent transamination of the resulting N-acyl-DAP. Interestingly, though the logic of lysine biosynthesis via meso-DAP is identical for most bacteria, different species selectively proceed via acetylation or succinylation of the meso-DAP, providing an opportunity to examine the differential activities and selectivity determinants of these potential antibiotic targets. We have characterized the meso-DAP acyltransferase and N-acyl-DAP aminotransferase enzymes from succinyl- and acetyl-utilizing species of bacteria involved in these steps, and have begun to delineate the sequence and structural features that distinguish these two classes of enzyme as well as uncovered a novel, broadly distributed class of meso-DAP acyltransferase involved in the biosynthesis of the β-lactam natural product tabtoxin.

Functional characterization of the early enzymes of lysine biosynthesis: Target-rich environment for antimicrobials

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.