An intramodular thioesterase domain catalyses chain release in the biosynthesis of a cytotoxic virulence factor.

ABSTRACT: An essential step in the biosynthesis of polyketide and non-ribosomal peptide natural products is cleavage of the thioester bond that tethers the acyl/peptidyl chain to its biosynthetic enzyme. In modular polyketide synthases (PKS) and non-ribosomal peptide synthetases (NRPS) chain release is typically catalysed by a single C-terminal thioesterase domain. A clear exception is the bimodular PKS-NRPS BurA that produces gonyol-an intermediate in the biosynthesis of the cytotoxic Burkholderia virulence factor malleicyprol. While BurA lacks a C-terminal thioesterase domain, making the mechanism by which gonyol is released unclear, it contains two uncommon non-C-terminal thioesterase domains: one at the N-terminus of module one (BurA TE-A) and one within module two (BurA TE-B). Here we sh

SUBMITTER: Little R 

PROVIDER: S-EPMC9428774 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature