Polyketide synthase chimeras reveal key role of ketosynthase domain in chain branching

October 19th, 2015 by Srividhya Sundaram

Nature Chemical Biology 11, 949 (2015). doi:10.1038/nchembio.1932

Authors: Srividhya Sundaram, Daniel Heine & Christian Hertweck

Biosynthesis of rhizoxin in Burkholderia rhizoxinica affords an unusual polyketide synthase module with ketosynthase and branching domains that install the δ-lactone, conferring antimitotic activity. To investigate their functions in chain branching, we designed chimeric modules with structurally similar domains from a glutarimide-forming module and a dehydratase. Biochemical, kinetic and mutational analyses reveal a structural role of the accessory domains and multifarious catalytic actions of the ketosynthase.

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