A Self‐Sacrificing <i>N</i>‐Methyltransferase Is the Precursor of the Fungal Natural Product Omphalotin
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- Sascha Ramm
- Institut für Chemie Strasse des 17. Juni 124 10623 Berlin Germany
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- Bartlomiej Krawczyk
- Institut für Chemie Strasse des 17. Juni 124 10623 Berlin Germany
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- Agnes Mühlenweg
- Institut für Chemie Strasse des 17. Juni 124 10623 Berlin Germany
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- Annette Poch
- Institut für Chemie Strasse des 17. Juni 124 10623 Berlin Germany
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- Eva Mösker
- Institut für Chemie Strasse des 17. Juni 124 10623 Berlin Germany
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- Roderich D. Süssmuth
- Institut für Chemie Strasse des 17. Juni 124 10623 Berlin Germany
抄録
<jats:title>Abstract</jats:title><jats:p>Research on ribosomally synthesized and posttranslationally modified peptides (RiPPs) has led to an increasing understanding of biosynthetic mechanisms, mostly drawn from bacterial examples. In contrast, reports on RiPPs from fungal producers, apart from the amanitins and phalloidins, are still scarce. The fungal cyclopeptide omphalotin A carries multiple N‐methylations on the peptide backbone, a modification previously known only from nonribosomal peptides. Mining the genome of the omphalotin‐producing fungus for a precursor peptide led to the identification of two biosynthesis genes, one encoding a methyltransferase OphMA that catalyzes the automethylation of its C‐terminus, which is then released and cyclized by the protease OphP. Our findings suggest a novel biosynthesis mechanism for a RiPP in which a modifying enzyme bears its own precursor peptide.</jats:p>
収録刊行物
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- Angewandte Chemie International Edition
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Angewandte Chemie International Edition 56 (33), 9994-9997, 2017-07-17
Wiley