Issue 11, 2018

Protein–protein interactions in polyketide synthase–nonribosomal peptide synthetase hybrid assembly lines

Abstract

Covering: up to early 2018

Polyketides and nonribosomal peptides are two major families of natural product with a broad range of biological activities. Polyketide synthases (PKSs) assemble small acetic acid-type acyl building blocks into polyketides through C–C bonds, and nonribosomal peptide synthetases (NRPSs) assemble amino acids into peptides through amide bonds. PKS–NRPS hybrid assembly lines build structurally complex polyketide–amino acid/peptide hybrid molecules that incorporate both acyl and aminoacyl building blocks into their products. Their combined functionalities expand the biological activities of these molecules by mixing their chemical properties. Protein–protein interactions are necessary within PKS–NRPS hybrid assembly lines to achieve accurate linkage between the PKS and NRPS systems. This review summarizes the current understanding of the roles and importance of the protein–protein interactions in various PKS–NRPS hybrid assembly lines.

Graphical abstract: Protein–protein interactions in polyketide synthase–nonribosomal peptide synthetase hybrid assembly lines

Article information

Article type
Review Article
Submitted
06 Mar 2018
First published
03 Aug 2018

Nat. Prod. Rep., 2018,35, 1185-1209

Protein–protein interactions in polyketide synthase–nonribosomal peptide synthetase hybrid assembly lines

A. Miyanaga, F. Kudo and T. Eguchi, Nat. Prod. Rep., 2018, 35, 1185 DOI: 10.1039/C8NP00022K

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements