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An Iterative Module in the Azalomycin F Polyketide Synthase Contains a Switchable Enoylreductase Domain
Author(s) -
Xu Wei,
Zhai Guifa,
Liu Yuanzhen,
Li Yuan,
Shi Yanrong,
Hong Kui,
Hong Hui,
Leadlay Peter F.,
Deng Zixin,
Sun Yuhui
Publication year - 2017
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201701220
Subject(s) - polyketide synthase , polyketide , dehydratase , modular design , biosynthesis , domain (mathematical analysis) , mutant , stereochemistry , computational biology , biology , chemistry , computer science , biochemistry , enzyme , programming language , mathematics , gene , mathematical analysis
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.

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