A dual transacylation mechanism for polyketide synthase chain release in enacyloxin antibiotic biosynthesis.

ABSTRACT: Polyketide synthases assemble diverse natural products with numerous important applications. The thioester intermediates in polyketide assembly are covalently tethered to acyl carrier protein domains of the synthase. Several mechanisms for polyketide chain release are known, contributing to natural product structural diversification. Here, we report a dual transacylation mechanism for chain release from the enacyloxin polyketide synthase, which assembles an antibiotic with promising activity against Acinetobacter baumannii. A non-elongating ketosynthase domain transfers the polyketide chain from the final acyl carrier protein domain of the synthase to a separate carrier protein, and a non-ribosomal peptide synthetase condensation domain condenses it with (1S,3R,4S)-3,4-dihydroxycyclohexane

SUBMITTER: Masschelein J 

PROVIDER: S-EPMC6774797 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature