| Autor: |
Wei Wang, Tianshun Hu, Frantom, Patrick A., Tianqing Zheng, Gerwe, Brian, del Amo, David Soriano, Garret, Sarah, Seidel III, Ronald D., Peng Wu |
| Předmět: |
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| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; 9/22/2009, Vol. 106 Issue 38, p16096-16101, 6p |
| Abstrakt: |
Lewis X (Lex)-containing glycans play important roles in numerous cellular processes. However, the absence of robust, facile, and cost-effective methods for the synthesis of Lex and its structurally related analogs has severely hampered the elucidation of the specific functions of these glycan epitopes. Here we demonstrate that chemically defined guanidine 5′-diphosphate-β-L-fucose (GDP- fucose), the universal fucosyl donor, the Lex trisaccharide, and their C-5 substituted derivatives can be synthesized on preparative scales, using a chemoenzymatic approach. This method exploits L-fucokinase/GDP-fucose pyrophosphorylase (FKP), a bifunctional enzyme isolated from Bacteroides fra gills 9343, which converts L-fucose into GDP-fucose via a fucose-1-phosphate (Fuc-1-P) inter- mediate. Combining the activities of FKP and a Helicobacterpylori α1,3 fucosyltransferase, we prepared a library of Lex trisaccharide glycans bearing a wide variety of functional groups at the fucose C-5 position. These neoglycoconjugates will be invaluable tools for studying Lex-mediated biological processes. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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