Title of article :
CST-II’s recognition domain for acceptor substrates in α-(2→8)-sialylations Original Research Article
Author/Authors :
Wenling Li، نويسنده , , Ping Zhang، نويسنده , , Amir J. Zuccolo، نويسنده , , Ruxiang Blake Zheng، نويسنده , , Chang-Chun Ling، نويسنده ,
Issue Information :
دوهفته نامه با شماره پیاپی سال 2011
Abstract :
CST-II is a bacterial sialyltransferase known for its ability to perform α-(2→8)-sialylations using GM3 related trisaccharide substrates. Previously, we probed the enzyme’s substrate specificity and developed an efficient synthesis for α-(2→8)-oligosialosides, and we suggested that CST-II could have a very small substrate recognition domain. Here we report our full studies on CST-II’s recognition feature for acceptor substrates. The current study further demonstrates the versatility of CST-II in preparing complex oligosaccharides that contain α-(2→8)-oligosialyl moieties.
Keywords :
Enzyme binding Site , Glycosylations , CST-II , Chemoenzymatic synthesis , ?-(2?8)-Sialylation
Journal title :
Carbohydrate Research
Journal title :
Carbohydrate Research