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

Sundaram S, Heine D, Hertweck C (2015) Polyketide synthase chimeras reveal key role of ketosynthase domain in chain branching. Nat Chem Biol 11(12), 949-951. PubMed

ILRS Authors

Christian Hertweck Srividhya Sundaram

Projects

Biochemical characterisation of bacterial terpene cyclases
Details

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.

Identifier

doi: 10.1038/nchembio.1932 PMID: 26479442

Go back