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In enzymology, a 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase (EC 2.4.1.152) is an enzyme that catalyzes the chemical reaction

GDP-beta-L-fucose + 1,4-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R ${\displaystyle \rightleftharpoons }$ GDP + 1,4-beta-D-galactosyl-(alpha-1,3-L-fucosyl)-N-acetyl-D-glucosaminyl- R

Thus, the two substrates of this enzyme are GDP-beta-L-fucose and 1,4-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R. Its 3 products are GDP, 1,4-beta-D-galactosyl-(alpha-1,3-L-fucosyl)-N-acetyl-D-glucosaminyl-, and R.

This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is GDP-beta-L-fucose:1,4-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-alpha-L-fucosyltransferase. Other names in common use include:

• Lewis-negative alpha-3-fucosyltransferase
• plasma alpha-3-fucosyltransferase
• guanosine diphosphofucose-glucoside alpha1→3-fucosyltransferase
• galactoside 3-fucosyltransferase
• GDP-L-fucose:1,4-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R
• 3-L-fucosyltransferase
• GDP-beta-L-fucose:1,4-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R, and
• 3-L-fucosyltransferase

This enzyme participates in 3 metabolic pathways: glycosphingolipid biosynthesis - neo-lactoseries, glycosphingolipid biosynthesis - globoseries, and glycan structures - biosynthesis 2.

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2NZW, 2NZX, and 2NZY.

References

• Johnson PH, Yates AD, Watkins WM (1981). "Human salivary fucosyltransferases : evidence for two distinct alpha-3-L-fucosyltransferase activities one or which is associated with the Lewis blood group Le gene". Biochem. Biophys. Res. Commun. 100 (4): 1611–8. doi:10.1016/0006-291X(81)90703-8. PMID 7295318.
• Schachter H, Narasimhan S, Gleeson P, Vella G (1983). "Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type". Biomembranes Part L: Membrane Biogenesis: Processing and Recycling. Methods in Enzymology. Vol. 98. pp. 98–134. doi:10.1016/0076-6879(83)98143-0. ISBN 978-0-12-181998-9. PMID 6366476.
• Ma B, Wang G, Palcic MM, Hazes B, Taylor DE (2003). "C-terminal amino acids of Helicobacter pylori alpha1,3/4 fucosyltransferases determine type I and type II transfer". J. Biol. Chem. 278 (24): 21893–900. doi:10.1074/jbc.M301704200. PMID 12676935.

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