- Source: Glycoprotein 3-alpha-L-fucosyltransferase
In enzymology, a 3/info/glycoprotein" target="_blank">glycoprotein 3-alpha-L-fucosyltransferase (EC 2.4.1.214) is an enzyme that catalyzes the chemical reaction
GDP-L-fucose + N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N- acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D- mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D- glucosaminyl}asparagine
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{\displaystyle \rightleftharpoons }
GDP + N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N- acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D- mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L- fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl}asparagine
The 5 substrates of this enzyme are GDP-L-fucose, [[N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-]], [[acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-]], [[mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-]], and [[glucosaminyl}asparagine]], whereas its 5 products are GDP, [[N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-]], [[acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-]], [[mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L-]], and [[fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl}asparagine]].
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is GDP-L-fucose:3/info/glycoprotein" target="_blank">glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-a cetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-man nosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glu cosaminyl}asparagine) 3-alpha-L-fucosyl-transferase. Other names in common use include GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,3-fucosyltransferase, GDP-L-Fuc:Asn-linked GlcNAc alpha1,3-fucosyltransferase, GDP-fucose:beta-N-acetylglucosamine (Fuc to, (Fucalpha1->6GlcNAc)-Asn-peptide) alpha1->3-fucosyltransferase, GDP-L-fucose:3/info/glycoprotein" target="_blank">glycoprotein (L-fucose to asparagine-linked, N-acetylglucosamine of, 4-N-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-, acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-, mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-, and glucosaminyl}asparagine) 3-alpha-L-fucosyl-transferase. This enzyme participates in glycan structures - biosynthesis 1.
References
Muller S, Hauser MT (2001). "Cloning and expression of cDNAs encoding alpha1,3-fucosyltransferase homologues from Arabidopsis thaliana". Biochim. Biophys. Acta. 1527 (1–2): 88–96. doi:10.1016/s0304-4165(01)00151-9. PMID 11420147.
Fabini G, Freilinger A, Altmann F, Wilson IB (2001). "Identification of core alpha 1,3-fucosylated glycans and cloning of the requisite fucosyltransferase cDNA from Drosophila melanogaster Potential basis of the neural anti-horseadish peroxidase epitope". J. Biol. Chem. 276 (30): 28058–67. doi:10.1074/jbc.M100573200. PMID 11382750.
Leiter H, Mucha J, Staudacher E, Grimm R, Glossl J, Altmann F (1999). "Purification, cDNA cloning, and expression of GDP-L-Fuc:Asn-linked GlcNAc alpha1,3-fucosyltransferase from mung beans". J. Biol. Chem. 274 (31): 21830–9. doi:10.1074/jbc.274.31.21830. PMID 10419500.
van Tetering A, Schiphorst WE, van den Eijnden DH, van Die I (1999). "Characterization of a core alpha1-->3-fucosyltransferase from the snail Lymnaea stagnalis that is involved in the synthesis of complex-type N-glycans". FEBS Lett. 461 (3): 311–4. doi:10.1016/S0014-5793(99)01489-1. PMID 10567717.
Staudacher E, Altmann F, Glössl J, März L, Schachter H, Kamerling JP, Hård K, Vliegenthart JF (1991). "GDP-fucose: beta-N-acetylglucosamine (Fuc to (Fuc alpha 1--6GlcNAc)-Asn-peptide)alpha 1--3-fucosyltransferase activity in honeybee (Apis mellifica) venom glands. The difucosylation of asparagine-bound N-acetylglucosamine". Eur. J. Biochem. 199 (3): 745–51. doi:10.1111/j.1432-1033.1991.tb16179.x. PMID 1868856.