Offloading Role of a Discrete Thioesterase in Type II Polyketide Biosynthesis

Author:

Hua Kangmin1,Liu Xiangyang12,Zhao Yuchun1,Gao Yaojie1,Pan Lifeng2,Zhang Haoran3,Deng Zixin1,Jiang Ming1ORCID

Affiliation:

1. State Key Laboratory of Microbial Metabolism, Joint International Research Laboratory of Metabolic & Developmental Sciences and School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, People’s Republic of China

2. State Key Laboratory of Bioorganic and Natural Products Chemistry, Center for Excellence in Molecular Synthesis, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Shanghai, People’s Republic of China

3. Department of Chemical and Biochemical Engineering, Rutgers, The State University of New Jersey, Piscataway, New Jersey, USA

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.

Funder

National science foundation of china

Publisher

American Society for Microbiology

Subject

Virology,Microbiology

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