Structural insights into dehydratase substrate selection for the borrelidin and fluvirucin polyketide synthases.

ABSTRACT: Engineered polyketide synthases (PKSs) are promising synthetic biology platforms for the production of chemicals with diverse applications. The dehydratase (DH) domain within modular type I PKSs generates an α,β-unsaturated bond in nascent polyketide intermediates through a dehydration reaction. Several crystal structures of DH domains have been solved, providing important structural insights into substrate selection and dehydration. Here, we present two DH domain structures from two chemically diverse PKSs. The first DH domain, isolated from the third module in the borrelidin PKS, is specific towards a trans-cyclopentane-carboxylate-containing polyketide substrate. The second DH domain, isolated from the first module in the fluvirucin B₁ PKS, accepts an amide-containing polyket

SUBMITTER: Barajas JF 

PROVIDER: S-EPMC6697708 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature