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Updated: Jun 25, 2025

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Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
Published on: September 28, 2022
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Kinetic Analysis of Lanthipeptide Cyclization by Substrate-Tolerant ProcM
Emily K Desormeaux1, Wilfred A van der Donk1,2
1Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, USA.
Biorxiv : the Preprint Server for Biology
|May 27, 2024
Summary
This study shows that modification rates can predict lanthipeptide ring patterns. However, these rates do not reliably predict the order of modifications for ProcM synthetase variants.
Area of Science:
- Biochemistry
- Molecular Biology
- Natural Product Synthesis
Background:
- Lanthipeptides are ribosomally synthesized peptides with thioether crosslinks.
- Class II lanthipeptide synthetases, like ProcM, perform complex post-translational modifications.
- ProcM exhibits broad substrate tolerance and high accuracy in forming (methyl)lanthionine rings.
Conclusions:
- The study confirms that modification rates are key determinants of the final lanthipeptide ring pattern.
- However, these rates are not consistently predictive of the modification order in ProcM variants.
- This highlights the complex interplay between substrate sequence, enzyme kinetics, and product formation in lanthipeptide biosynthesis.
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