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NatureasStereochemist:Unravelingthecomplexitiesofpolyketideantibioticbiosynthesis

来源:bet9九州最新官网 发布时间 :2011-04-07  阅读次数 :1191

报告题目:Nature as Stereochemist: Unraveling the complexities of polyketide antibiotic biosynthesis
报? 告? 人:David Cane, Professor
Department of Chemistry,
Brown University, Providence, RI 02912-9108 USA
Email: This e-mail address is being protected from spambots. You need JavaScript enabled to view it.
报告时间:4月11日 上午9:30
报告地点:徐汇校区哲生馆112会议室
组织单位:分子微生物代谢实验室

Abstract

Polyketide synthases are responsible for the biosynthesis of complex antibiotics. In modular polyketide synthases, individual modules carry out a single round of polyketide chain elongation, with the required modifications of functionality and stereochemistry being controlled by dedicated protein domains such as ketoreductase (KR), dehydratase (DH), and enoylreductase (ER) domains. All of the intermediates remain covalently bound to acyl carrier protein (ACP) domains until the release of the final product by a dedicated thioesterase (TE) domain.? By using varying combinations of individual recombinant protein domains, it has become possible to dissect polyketide biosynthesis into its component steps and analyze each discrete reaction.

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