期刊
NATURE PROTOCOLS
卷 5, 期 4, 页码 636-646出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nprot.2010.3
关键词
-
资金
- National Cancer Institute [R01 CA118208]
- NSF [CHE-0616892]
- NIH [R01 AI083754, R01 HD061935, R01 GM085267]
- China Scholarship Council
- EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT [R01HD061935] Funding Source: NIH RePORTER
- NATIONAL CANCER INSTITUTE [R01CA118208] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI083754] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM085267] Funding Source: NIH RePORTER
Enzymatic synthesis using glycosyltransferases is a powerful approach to building polysaccharides with high efficiency and selectivity. Sugar nucleotides are fundamental donor molecules in enzymatic glycosylation reactions by Leloir-type glycosyltransferases. The applications of these donors are restricted by their limited availability. In this protocol, N-acetylglucosamine (GlcNAc)/N-acetylgalactosamine (GalNAc) are phosphorylated by N-acetylhexosamine 1-kinase (NahK) and subsequently pyrophosphorylated by N-acetylglucosamine uridyltransferase (GlmU) to give UDP-GlcNAc/GalNAc. Other UDP-GlcNAc/GalNAc analogues can also be prepared depending on the tolerance of these enzymes to the modified sugar substrates. Starting from l-fucose, GDP-fucose is constructed by one bifunctional enzyme l-fucose pyrophosphorylase (FKP) via two reactions.
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