學術報告-NatureasStereochemist:Unravelingthecomplexitiesofpolyketideantibioticbiosynthesis
發布時間 :2011-04-07  閱讀次數 :2992

報告題目:Nature as Stereochemist: Unraveling the complexities of polyketide antibiotic biosynthesis
報  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.
報告時間👱‍♀️:4月11日 上午9:30
報告地點:徐匯校區哲生館112會議室
組織單位:分子微生物代謝實驗室

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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