Diversity of nature's assembly lines: Recent discoveries in non-ribosomal peptide synthesis

Jennifer A. E. Payne, Melanie Schoppet, Mathias Henning Hansen, Max J. Cryle

Research output: Contribution to journalReview ArticleOtherpeer-review

64 Citations (Scopus)


The biosynthesis of complex natural products by non-ribosomal peptide synthetases (NRPSs) and the related polyketide synthases (PKSs) represents a major source of important bioactive compounds. These large, multi-domain machineries are able to produce a fascinating range of molecules due to the nature of their modular architectures, which allows natural products to be assembled and tailored in a modular, step-wise fashion. In recent years there has been significant progress in characterising the important domains and underlying mechanisms of non-ribosomal peptide synthesis. More significantly, several studies have uncovered important examples of novel activity in many NRPS domains. These discoveries not only greatly increase the structural diversity of the possible products of NRPS machineries but-possibly more importantly-they improve our understanding of what is a highly important, yet complex, biosynthetic apparatus. In this review, several recent examples of novel NRPS function will be introduced, which highlight the range of previously uncharacterised activities that have now been detected in the biosynthesis of important natural products by these mega-enzyme synthetases.

Original languageEnglish
Pages (from-to)9-22
Number of pages14
JournalMolecular BioSystems
Issue number1
Publication statusPublished - 2017

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