3D model (Jmol)
|Supplementary data page|
|Refractive index (n),
Dielectric constant (εr), etc.
|UV, IR, NMR, MS|
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
|what is ?)(|
Fucose is a hexose deoxy sugar with the chemical formula C6H12O5. It is found on N-linked glycans on the mammalian, insect and plant cell surface, and is the fundamental sub-unit of the fucoidan polysaccharide. α(1→3) linked core fucose is a suspected carbohydrate antigen for IgE-mediated allergy.
Two structural features distinguish fucose from other six-carbon sugars present in mammals: the lack of a hydroxyl group on the carbon at the 6-position (C-6) (thereby making it a deoxy sugar) and the L-configuration. It is equivalent to 6-deoxy-L-galactose.
In the fucose-containing glycan structures, fucosylated glycans, fucose can exist as a terminal modification or serve as an attachment point for adding other sugars. In human N-linked glycans, fucose is most commonly linked α-1,6 to the reducing terminal β-N-acetylglucosamine. However, fucose at the non-reducing termini linked α-1,2 to galactose forms the H antigen, the substructure of the A and B blood group antigens.
Fucose is released from fucose-containing polymers by an enzyme called α-fucosidase.
L-Fucose is claimed to have application in cosmetics, pharmaceuticals, and dietary supplements. However, these claims are often not supported by peer-reviewed scientific studies.
Fucosylation of antibodies has been established to reduce binding to the Fc receptor of Natural Killer cells and thereby reduce antigen-dependent cellular cytotoxicity. Therefore therapeutic antibodies that are designed to recruit the immune system to cancers cells have been manufactured in cell lines deficient in the enzyme for core fucosylation (FUT8) and thereby enhancing the in vivo cell killing.
- Daniel J. Becker; John B. Lowe (July 2003). "Fucose: biosynthesis and biological function in mammals". Glycobiology. 13 (7): 41R–53R. doi:10.1093/glycob/cwg054. PMID 12651883.
- Daniel J. Moloney; Robert S. Haltiwanger (July 1999). "The O-linked fucose glycosylation pathway: identification and characterization of a uridine diphosphoglucose: fucose-[beta]1,3-glucosyltransferase activity from Chinese hamster ovary cells". Glycobiology. 9 (7): 679–687. doi:10.1093/glycob/9.7.679. PMID 10362837.
- Dalziel, Martin; Crispin, Max; Scanlan, Christopher N.; Zitzmann, Nicole; Dwek, Raymond A. (2014-01-03). "Emerging Principles for the Therapeutic Exploitation of Glycosylation". Science. 343 (6166): 1235681. doi:10.1126/science.1235681. ISSN 0036-8075. PMID 24385630.