An Iterative Module in the Azalomycin F Polyketide Synthase Contains a Switchable Enoylreductase Domain.

Authors
Xu, Wei 
Zhai, Guifa 
Liu, Yuanzhen 
Li, Yuan 
Shi, Yanrong 

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Type
Article
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Abstract

Detailed analysis of the modular Type I polyketide synthase (PKS) involved in the biosynthesis of the marginolactone azalomycin F in mangrove Streptomyces sp. 211726 has shown that only nineteen extension modules are required to accomplish twenty cycles of polyketide chain elongation. Analysis of the products of a PKS mutant specifically inactivated in the dehydratase domain of extension-module 1 showed that this module catalyzes two successive elongations with different outcomes. Strikingly, the enoylreductase domain of this module can apparently be "toggled" off and on : it functions in only the second of these two cycles. This novel mechanism expands our understanding of PKS assembly-line catalysis and may explain examples of apparent non-colinearity in other modular PKS systems.

Publication Date
2017-05-08
Online Publication Date
2017-04-18
Acceptance Date
Keywords
antibiotics, biosynthesis, enoylreductases, iteration modules, macrocyclic polyketides, Macrolides, Molecular Conformation, Mutation, Oxidoreductases, Polyketide Synthases
Journal Title
Angew Chem Int Ed Engl
Journal ISSN
1433-7851
1521-3773
Volume Title
56
Publisher
Wiley
Rights
Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
Sponsorship
Biotechnology and Biological Sciences Research Council (BB/I002413/1)