ArticleJournal of the American Chemical Society2025
Peptide Prenylation Follows Divergent Substrate Engagement Rules.
Article in Journal of the American Chemical Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
1 citing paper in PubMed.
- Enzymatic Prenylation of Proteins and Peptides: From Cysteine S-Prenylation to Tryptophan-Selective Biocatalysis.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
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Authors and funding
3 authors.
Funding
Abstract
Lipidation of ribosomally synthesized and post-translationally modified peptides (RiPPs) is a bioactivity conferring modification. In this study, we present evidence that prenylation of lanthipeptides─a widely distributed chemical family of RiPPs─proceeds with lanthipeptide prenyltransferases recognizing the entirety of the peptidic substrate including the N-terminal leader region of the RiPP precursor peptide. This mode of substrate recognition is markedly different from that of prenyltransferases that lipidate other RiPPs such as cyanobactins wherein the leader peptide is not engaged at all. Molecular recognition rules dictate catalysis, and we posit that leader peptide recognition imposes substrate selectivity upon lanthipeptide prenyltransferases and narrows their substrate scope as compared to the leader-free prenylation of cyanobactins which proceeds in a hyperpromiscuous manner.
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