4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase

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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 $\rightleftharpoons$ 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, whereas 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

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

[edit] References

IUBMB entry for 2.4.1.152
BRENDA references for 2.4.1.152 (Recommended.)
PubMed references for 2.4.1.152
PubMed Central references for 2.4.1.152
Google Scholar references for 2.4.1.152
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: 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". Methods. Enzymol. 98: 98–134. 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: 21893–900. doi:10.1074/jbc.M301704200. PMID 12676935.