Angewandte Chemie - International Edition
Angewandte Chemie - International Edition
5 years ago

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

An Iterative Module in the Azalomycin F Polyketide Synthase Contains a Switchable Enoylreductase Domain
Yuanzhen Liu, Peter F. Leadlay, Guifa Zhai, Yanrong Shi, Kui Hong, Zixin Deng, Wei Xu, Yuhui Sun, Hui Hong, Yuan Li
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. Off and On: The azalomycin F biosynthetic pathway contains a switchable enoylreductase (ER) domain in an iterative polyketide synthase (PKS) module for polyketide backbone elongations. The ER domain is toggled from non-functional (“off”, black) in the first extension process to functional (“on”, red) in the second. LM=loading module.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/anie.201701220

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