Exploiting the Reversibility of Natural Product Glycosyltransferase-Catalyzed Reactions
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- Changsheng Zhang
- Laboratory for Biosynthetic Chemistry, Pharmaceutical Sciences Division, School of Pharmacy, National Cooperative Drug Discovery Group Program, University of Wisconsin (UW)–Madison, 777 Highland Avenue, Madison, WI 53705–2222, USA.
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- Byron R. Griffith
- Laboratory for Biosynthetic Chemistry, Pharmaceutical Sciences Division, School of Pharmacy, National Cooperative Drug Discovery Group Program, University of Wisconsin (UW)–Madison, 777 Highland Avenue, Madison, WI 53705–2222, USA.
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- Qiang Fu
- Laboratory for Biosynthetic Chemistry, Pharmaceutical Sciences Division, School of Pharmacy, National Cooperative Drug Discovery Group Program, University of Wisconsin (UW)–Madison, 777 Highland Avenue, Madison, WI 53705–2222, USA.
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- Christoph Albermann
- Laboratory for Biosynthetic Chemistry, Pharmaceutical Sciences Division, School of Pharmacy, National Cooperative Drug Discovery Group Program, University of Wisconsin (UW)–Madison, 777 Highland Avenue, Madison, WI 53705–2222, USA.
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- Xun Fu
- Laboratory for Biosynthetic Chemistry, Pharmaceutical Sciences Division, School of Pharmacy, National Cooperative Drug Discovery Group Program, University of Wisconsin (UW)–Madison, 777 Highland Avenue, Madison, WI 53705–2222, USA.
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- In-Kyoung Lee
- Laboratory for Biosynthetic Chemistry, Pharmaceutical Sciences Division, School of Pharmacy, National Cooperative Drug Discovery Group Program, University of Wisconsin (UW)–Madison, 777 Highland Avenue, Madison, WI 53705–2222, USA.
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- Lingjun Li
- Laboratory for Biosynthetic Chemistry, Pharmaceutical Sciences Division, School of Pharmacy, National Cooperative Drug Discovery Group Program, University of Wisconsin (UW)–Madison, 777 Highland Avenue, Madison, WI 53705–2222, USA.
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- Jon S. Thorson
- Laboratory for Biosynthetic Chemistry, Pharmaceutical Sciences Division, School of Pharmacy, National Cooperative Drug Discovery Group Program, University of Wisconsin (UW)–Madison, 777 Highland Avenue, Madison, WI 53705–2222, USA.
抄録
<jats:p>Glycosyltransferases (GTs), an essential class of ubiquitous enzymes, are generally perceived as unidirectional catalysts. In contrast, we report that four glycosyltransferases from two distinct natural product biosynthetic pathways—calicheamicin and vancomycin—readily catalyze reversible reactions, allowing sugars and aglycons to be exchanged with ease. As proof of the broader applicability of these new reactions, more than 70 differentially glycosylated calicheamicin and vancomycin variants are reported. This study suggests the reversibility of GT-catalyzed reactions may be general and useful for generating exotic nucleotide sugars, establishing in vitro GT activity in complex systems, and enhancing natural product diversity.</jats:p>
収録刊行物
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- Science
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Science 313 (5791), 1291-1294, 2006-09
American Association for the Advancement of Science (AAAS)
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詳細情報 詳細情報について
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- CRID
- 1364233269943345152
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- NII論文ID
- 80018957813
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- ISSN
- 10959203
- 00368075
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- データソース種別
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