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

Abstract

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
Volume13
Issue number1
DOIs
Publication statusPublished - 2017

Cite this

@article{4469c2329eec432c87b954b910568942,
title = "Diversity of nature's assembly lines: Recent discoveries in non-ribosomal peptide synthesis",
abstract = "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.",
author = "Payne, {Jennifer A. E.} and Melanie Schoppet and Hansen, {Mathias Henning} and Cryle, {Max J.}",
year = "2017",
doi = "10.1039/c6mb00675b",
language = "English",
volume = "13",
pages = "9--22",
journal = "Molecular BioSystems",
issn = "1742-206X",
publisher = "The Royal Society of Chemistry",
number = "1",

}

Diversity of nature's assembly lines : Recent discoveries in non-ribosomal peptide synthesis. / Payne, Jennifer A. E.; Schoppet, Melanie; Hansen, Mathias Henning; Cryle, Max J.

In: Molecular BioSystems, Vol. 13, No. 1, 2017, p. 9-22.

Research output: Contribution to journalReview ArticleOtherpeer-review

TY - JOUR

T1 - Diversity of nature's assembly lines

T2 - Recent discoveries in non-ribosomal peptide synthesis

AU - Payne, Jennifer A. E.

AU - Schoppet, Melanie

AU - Hansen, Mathias Henning

AU - Cryle, Max J.

PY - 2017

Y1 - 2017

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85006931155&partnerID=8YFLogxK

U2 - 10.1039/c6mb00675b

DO - 10.1039/c6mb00675b

M3 - Review Article

VL - 13

SP - 9

EP - 22

JO - Molecular BioSystems

JF - Molecular BioSystems

SN - 1742-206X

IS - 1

ER -