Reprogramming of the Aurantinin Polyketide Assembly Line to Synthesize Auritriacids by Excising an Atypical Enoyl-CoA Hydratase Domain.

ABSTRACT: Modular polyketide synthases (PKSs) are capable of synthesizing diverse natural products with fascinating bioactivities. Canonical enoyl-CoA hydratases (ECHs) are components of the β-branching cassette that modifies the polyketide chain by adding a β-methyl branch. Herein, it is demonstrated that the deletion of an atypical ECH_Q domain (featuring a Q²⁸⁰ residue) of Art21, a didomain protein contains an ECH_Q domain and a thioesterase (TE) domain, reprograms the polyketide assembly line from synthesizing tetracyclic aurantinins (ARTs) to bicyclic auritriacids (ATAs) with much lower antibacterial activities. Genes encoding the ECH_Q-TE didomain proteins distribute in many PKS gene clusters from different bacteria. Significantly, the ART PKS machinery

SUBMITTER: Wang D 

PROVIDER: S-EPMC11425284 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature