- Source: 3-Galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase
In enzymology, a 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase (EC 2.4.1.65) is an enzyme that catalyzes the chemical reaction
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-D-glucosaminyl-R
⇌
{\displaystyle \rightleftharpoons }
GDP + beta-D-galactosyl-(1->3)-[alpha-L-fucosyl-(1->4)]-N-acetyl-beta-D- glucosaminyl-R
Thus, the two substrates of this enzyme are GDP-beta-L-fucose and [[beta-D-galactosyl-(1->3)-N-acetyl-D-glucosaminyl-R]], whereas its 3 products are GDP, [[beta-D-galactosyl-(1->3)-[alpha-L-fucosyl-(1->4)]-N-acetyl-beta-D-]], and glucosaminyl-R.
This enzyme participates in 3 metabolic pathways: glycosphingolipid biosynthesis - lactoseries, glycosphingolipid biosynthesis - neo-lactoseries, and glycan structures - biosynthesis 2.
Nomenclature
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is GDP-L-fucose:3-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R 4I-alpha-L-fucosyltransferase. Other names in common use include:
References
Prieels JP, Monnom D, Dolmans M, Beyer TA, Hill RL (October 1981). "Co-purification of the Lewis blood group N-acetylglucosaminide alpha 1 goes to 4 fucosyltransferase and an N-acetylglucosaminide alpha 1 goes to 3 fucosyltransferase from human milk". The Journal of Biological Chemistry. 256 (20): 10456–63. PMID 7287719.
Rasko DA, Wang G, Palcic MM, Taylor DE (February 2000). "Cloning and characterization of the alpha(1,3/4) fucosyltransferase of Helicobacter pylori". The Journal of Biological Chemistry. 275 (7): 4988–94. doi:10.1074/jbc.275.7.4988. PMID 10671538.
Wilson IB (June 2001). "Identification of a cDNA encoding a plant Lewis-type alpha1,4-fucosyltransferase". Glycoconjugate Journal. 18 (6): 439–47. doi:10.1023/A:1016030000527. PMID 12084979.
Ma B, Wang G, Palcic MM, Hazes B, Taylor DE (June 2003). "C-terminal amino acids of Helicobacter pylori alpha1,3/4 fucosyltransferases determine type I and type II transfer". The Journal of Biological Chemistry. 278 (24): 21893–900. doi:10.1074/jbc.M301704200. PMID 12676935.