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Glycobiology Advance Access published online on September 14, 2006
Glycobiology, doi:10.1093/glycob/cwl040
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© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org
Received June 21, 2006
Revised August 25, 2006
Accepted August 25, 2006

Article

Fucosylation in Prokaryotes and Eukaryotes

Bing Ma 1, Joanne L. Simala-Grant 1, and Diane E. Taylor 1 *

1 Department of Medical Microbiology and Immunology University of Alberta, Edmonton, Alberta, T6G 2H7 Canada

* To whom correspondence should be addressed.
Diane E. Taylor, E-mail: diane.taylor{at}ualberta.ca


  Abstract

Fucosylated carbohydrate structures are involved in a variety of biological and pathological processes in eukaryotic organisms including tissue development, angiogenesis, fertilization, cell adhesion, inflammation and tumor metastasis. In contrast, fucosylation appears less common in prokaryotic organisms and has been suggested to be involved in molecular mimicry, adhesion, colonization and modulating the host immune response. Fucosyltransferases, present in both eukaryotic and prokaryotic organisms, are the enzymes responsible for the catalysis of fucose transfer from donor guanosine-diphosphate fucose to various acceptor molecules including oligosaccharides, glycoproteins and glycolipids. To date, several subfamilies of mammalian fucosyltransferases have been well characterized; these enzymes are therefore delineated and used as models. Non-mammalian fucosyltransferases that possess different domain construction or display distinctive acceptor substrate specificity are highlighted. It is noteworthy that the glycoconjugates from plants and schistosomes contain some unusual fucose linkages, suggesting the presence of novel fucosyltransferase subfamilies as yet to be characterized. Despite the very low sequence homology, striking functional similarity is exhibited between mammalian and Helicobacter pylori {alpha}1,3/4 fucosyltransferases, implying these enzymes likely share a conserved mechanistic and structural basis for fucose transfer; such conserved functional features might also exist when comparing other FucT subfamilies from different origins. Fucosyltranferases are promising tools used in synthesis of fucosylated oligosaccharides and glycoconjugates, which show great potential in the treatment of infectious and inflammatory diseases and tumor metastasis.

Keywords: Eukaryotes/FucTs/Fucosylation/Prokaryotes.
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