2016年9月
A Lanthipeptide-like N-Terminal Leader Region Guides Peptide Epimerization by Radical SAM Epimerases: Implications for RiPP Evolution
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
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- 巻
- 55
- 号
- 40
- 開始ページ
- 12330
- 終了ページ
- 12333
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1002/anie.201602863
- 出版者・発行元
- WILEY-V C H VERLAG GMBH
Ribosomally synthesized and posttranslationally modified peptide natural products (RiPPs) exhibit diverse structures and bioactivities and are classified into distinct biosynthetic families. A recently reported family is the proteusins, with the prototype members polytheonamides being generated by almost 50 maturation steps, including introduction of D-residues at multiple positions by an unusual radical SAM epimerase. A region in the protein-like N-terminal leader of proteusin precursors is identified that is crucial for epimerization. It resembles a precursor motif previously shown to mediate interaction in thioether bridge-formation in class I lanthipeptide biosynthesis. Beyond this region, similarities were identified between proteusin and further RiPP families, including class I lanthipeptides. The data suggest that common leader features guide distinct maturation types and that nitrile hydratase-like enzymes are ancestors of several RiPP classes.
- リンク情報
- ID情報
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- DOI : 10.1002/anie.201602863
- ISSN : 1433-7851
- eISSN : 1521-3773
- PubMed ID : 27584723
- Web of Science ID : WOS:000384713700032