Probing the Aglycon Promiscuity of an Engineered Glycosyltransferase

被引:112
作者
Gantt, Richard W. [1 ]
Goff, Randal D. [1 ]
Williams, Gavin J. [1 ]
Thorson, Jon S. [1 ]
机构
[1] Univ Wisconsin, Sch Pharm, Lab Biosynthet Chem, UW Natl Cooperat Drug Discovery Grp, Madison, WI 53705 USA
基金
美国国家卫生研究院;
关键词
carbohydrates; enzymes; glycosides; glycosylation; natural products;
D O I
10.1002/anie.200803508
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
(Figure Presented) A sweet library: Two variants (wild-type (WT) and a triple mutant) of glycosyltransferase (GT) OleD have been shown to catalyze glycosylation of over 70 substrates, formation of O-, S- and N-glycosidic bonds, and iterative glycosylation (see scheme). Identified substrates include nucleophiles not previously known to act in GT reactions and span numerous natural product and therapeutic drug classes. © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.
引用
收藏
页码:8889 / 8892
页数:4
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