期刊
NATURE CHEMICAL BIOLOGY
卷 6, 期 5, 页码 321-323出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nchembio.343
关键词
-
资金
- UK Engineering and Physical Sciences Research Council [EP/D059186/1]
- UK Medical Research Council [G0701861]
- Leverhulme Trust [RF/4/RFG/2008/0544]
- Danish Agency for Science, Technology and Innovation [272-08-0449]
- Engineering and Physical Sciences Research Council [EP/D059186/1] Funding Source: researchfish
- Medical Research Council [G0701861] Funding Source: researchfish
- EPSRC [EP/D059186/1] Funding Source: UKRI
- MRC [G0701861] Funding Source: UKRI
Glycosyltransferases are carbohydrate-active enzymes with essential roles in numerous important biological processes. We have developed a new donor analog for galactosyltransferases that locks a representative target enzyme in a catalytically inactive conformation, thus almost completely abolishing sugar transfer. Results with other galactosyltransferases suggest that this unique mode of glycosyltransferase inhibition may also be generally applicable to other members of this important enzyme family.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据