Offloading Role of a Discrete Thioesterase in Type II Polyketide Biosynthesis.

ABSTRACT: Type II polyketides are a group of secondary metabolites with various biological activities. In nature, biosynthesis of type II polyketides involves multiple enzymatic steps whereby key enzymes, including ketoacyl-synthase (KS_α), chain length factor (KS_β), and acyl carrier protein (ACP), are utilized to elongate the polyketide chain through a repetitive condensation reaction. During each condensation, the biosynthesis intermediates are covalently attached to KS_α or ACP via a thioester bond and are then cleaved to release an elongated polyketide chain for successive postmodification. Despite its critical role in type II polyketide biosynthesis, the enzyme and its corresponding mechanism for type II polyketide chain release through thioester bond breakage hav

SUBMITTER: Hua K 

PROVIDER: S-EPMC7492732 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature