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Chemoenzymatic synthesis of GDP-L-fucose and the Lewis X glycan derivatives

Academic Article
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Overview

authors

  • Wang, W.
  • Hu, T.
  • Frantom, P. A.
  • Zheng, T.
  • Gerwe, B.
  • Soriano del Amo, D.
  • Garret, S.
  • Seidel III, R. D.
  • Wu, Peng

publication date

  • September 2009

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • Lewis X (Le(x))-containing glycans play important roles in numerous cellular processes. However, the absence of robust, facile, and cost-effective methods for the synthesis of Le(x) 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-beta-l-fucose (GDP-fucose), the universal fucosyl donor, the Le(x) 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 fragilis 9343, which converts l-fucose into GDP-fucose via a fucose-1-phosphate (Fuc-1-P) intermediate. Combining the activities of FKP and a Helicobacter pylori alpha1,3 fucosyltransferase, we prepared a library of Le(x) trisaccharide glycans bearing a wide variety of functional groups at the fucose C-5 position. These neoglycoconjugates will be invaluable tools for studying Le(x)-mediated biological processes.

subject areas

  • Adenosine Triphosphate
  • Antigens, CD15
  • Bacterial Proteins
  • Bacteroides fragilis
  • Catalysis
  • Crystallography, X-Ray
  • Electrophoresis, Polyacrylamide Gel
  • Guanosine Diphosphate Fucose
  • Guanosine Triphosphate
  • Humans
  • Kinetics
  • Magnetic Resonance Spectroscopy
  • Molecular Structure
  • Nucleotidyltransferases
  • Phosphotransferases (Alcohol Group Acceptor)
  • Polysaccharides
  • Substrate Specificity
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Research

keywords

  • catalysis
  • enzyme
  • glycobiology
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Identity

PubMed Central ID

  • PMC2752511

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.0908248106

PubMed ID

  • 19805264
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Additional Document Info

start page

  • 16096

end page

  • 16101

volume

  • 106

issue

  • 38

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