ArticleJournal of the American Chemical Society2026
Microbial dl-Peptidases Enable Predator Defense and Facilitate Structure Elucidation of Complex Natural Products.
Article in Journal of the American Chemical Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Synthetic microbial communities: emerging live biotherapeutics for targeted gut microbiome modulation.Gut microbes · 2026Review
- Structural and Functional Siderophore Remodeling by Enzymatic Delipidation.Angewandte Chemie (International ed. in English) · 2026Article
- Synthetic microbial communities for studying the fate and ecological role of specialized metabolites.Essays in biochemistry · 2026Review
- When neighbors control metabolite fate: consequences for plant pathogen virulence and biocontrol outcomes.Applied and environmental microbiology · 2026Article
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Authors and funding
12 authors.
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Abstract
Peptidases are indispensable tools in biotechnology and chemical biology. However, the enzyme repertoire for the selective hydrolysis of dl-amide bonds in peptides is small. Here, we describe novel dl-peptidases that mediate complex microbial interactions. These enzymes, Lip3 and Lip7, convert lipopeptides into potent amoebicidal agents via selective dl-peptide bond cleavage. Using structural analyses and mutagenesis, we identified an unusual Ser-Lys-Lys-Tyr catalytic tetrad required for dl-specificity. Despite their high structural similarity, both enzymes show distinct substrate preferences: Lip3 acts primarily as a carboxypeptidase, removing a single C-terminal residue, while Lip7 excises a tripeptide. Although their substrate scopes are broad, they are highly specific with regard to their respective cutting sites. These features make these dl-peptidases powerful tools for elucidating the structure of complex peptide-based natural products, including tensin and WLIP. Overall, this work elucidates the molecular mechanisms of cooperative microbial defense and provides a new enzymatic toolbox for biocatalysis and natural product discovery.
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