Ramm_2017_Angew.Chem.Int.Ed.Engl_56_9994

Reference

Title : A Self-Sacrificing N-Methyltransferase Is the Precursor of the Fungal Natural Product Omphalotin - Ramm_2017_Angew.Chem.Int.Ed.Engl_56_9994
Author(s) : Ramm S , Krawczyk B , Muhlenweg A , Poch A , Mosker E , Sussmuth RD
Ref : Angew Chem Int Ed Engl , 56 :9994 , 2017
Abstract :

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 omphalotinA 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.

PubMedSearch : Ramm_2017_Angew.Chem.Int.Ed.Engl_56_9994
PubMedID: 28715095
Gene_locus related to this paper: ompol-OphP

Citations formats

Ramm S, Krawczyk B, Muhlenweg A, Poch A, Mosker E, Sussmuth RD (2017)
A Self-Sacrificing N-Methyltransferase Is the Precursor of the Fungal Natural Product Omphalotin
Angew Chem Int Ed Engl 56 :9994

Ramm S, Krawczyk B, Muhlenweg A, Poch A, Mosker E, Sussmuth RD (2017)
Angew Chem Int Ed Engl 56 :9994