Polyketide synthase chimeras reveal key role of ketosynthase domain in chain branching.
(2015) Polyketide synthase chimeras reveal key role of ketosynthase domain in chain branching. Nat Chem Biol 11(12), 949-951. PubMed
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Biochemical characterisation of bacterial terpene cyclases
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Abstract
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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doi: 10.1038/nchembio.1932 PMID: 26479442
