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Updated: May 7, 2026
11:32
A Hydrogen-Deuterium Exchange Mass Spectrometry (HDX-MS) Platform for Investigating Peptide Biosynthetic Enzymes
Published on: May 4, 2020
Insights into the evolution of lanthipeptide biosynthesis.
Yi Yu1, Qi Zhang, Wilfred A van der Donk
1Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, 61801.
Protein Science : a Publication of the Protein Society
|September 17, 2013
Summary
Lanthipeptides are complex natural products with multiple thioether crosslinks. This review explores the evolutionary pathways of lanthipeptide biosynthetic enzymes using genomic data.
Area of Science:
- Biochemistry
- Molecular Biology
- Natural Product Chemistry
Background:
- Lanthipeptides are a class of post-translationally modified peptides.
- They are characterized by multiple thioether crosslinks formed via unique biochemical reactions.
- Multiple distinct biosynthetic pathways for lanthipeptides have evolved.
Purpose of the Study:
- To review the evolution of lanthipeptide biosynthetic enzymes.
- To present a model for enzyme evolution based on current genomic data.
- To highlight the efficiency and evolvability of lanthipeptide biosynthesis.
Main Methods:
- Analysis of genomic information.
- Review of existing literature on lanthipeptide biosynthesis.
- Development of an evolutionary model for lanthipeptide enzymes.
Main Results:
- Genomic data provides insights into the evolution of lanthipeptide pathways.
- A model for the evolution of lanthipeptide biosynthetic enzymes has been proposed.
- The post-translational modification route is highly efficient and evolvable.
Conclusions:
- The study discusses a model for the evolution of lanthipeptide biosynthetic enzymes.
- Understanding these evolutionary pathways offers insights into natural product biosynthesis.
- Further genomic exploration will continue to illuminate these processes.
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