Offloading Role of a Discrete Thioesterase in Type II Polyketide Biosynthesis
Kangmin Hua, Xiangyang Liu, Yuchun Zhao, Yaojie Gao, Lifeng Pan, Haoran Zhang, Zixin Deng, Ming Sen Jiang
Abstract
Kangmin Hua, Xiangyang Liu, Yuchun Zhao, Yaojie Gao, Lifeng Pan, Haoran Zhang, Zixin Deng, Ming Sen Jiang
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.
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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.
Key concepts: Polyketide, Acyl carrier protein, Biosynthesis, Thioester, Polyketide synthase, Thioesterase, Chemistry, Enzyme