Vinylogous Dehydration by a Polyketide Dehydratase Domain in Curacin Biosynthesis.

ABSTRACT: Polyketide synthase (PKS) enzymes continue to hold great promise as synthetic biology platforms for the production of novel therapeutic agents, biofuels, and commodity chemicals. Dehydratase (DH) catalytic domains play an important role during polyketide biosynthesis through the dehydration of the nascent polyketide intermediate to provide olefins. Our understanding of the detailed mechanistic and structural underpinning of DH domains that control substrate specificity and selectivity remains limited, thus hindering our efforts to rationally re-engineer PKSs. The curacin pathway houses a rare plurality of possible double bond permutations containing conjugated olefins as well as both cis- and trans-olefins, providing an unrivaled model system for polyketide dehydration. All four DH domains

SUBMITTER: Fiers WD 

PROVIDER: S-EPMC5590676 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature