Enzymes
| UniProtKB help_outline | 76 proteins |
Reaction participants Show >> << Hide
- Name help_outline a neolactoside nLc6Cer(d18:1(4E)) Identifier CHEBI:61610 Charge 0 Formula C59H102N3O33R SMILEShelp_outline [C@H]1(O[C@@H]([C@H](O)[C@@H]([C@H]1O)O[C@@H]2O[C@H](CO)[C@H]([C@@H]([C@H]2NC(C)=O)O)O[C@@H]3O[C@@H]([C@H](O)[C@@H]([C@H]3O)O)CO)CO)O[C@H]4[C@@H]([C@@H](NC(C)=O)[C@H](O[C@@H]5[C@H]([C@H](O[C@H]6[C@@H]([C@H]([C@H](OC[C@@H]([C@@H](/C=C/CCCCCCCCCCCCC)O)NC(*)=O)O[C@@H]6CO)O)O)O[C@@H]([C@@H]5O)CO)O)O[C@@H]4CO)O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline GDP-β-L-fucose Identifier CHEBI:57273 (Beilstein: 9178112) help_outline Charge -2 Formula C16H23N5O15P2 InChIKeyhelp_outline LQEBEXMHBLQMDB-JGQUBWHWSA-L SMILEShelp_outline C[C@@H]1O[C@H](OP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c2nc(N)[nH]c3=O)[C@@H](O)[C@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 67 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a neolactoside III3-α-Fuc-nLc6Cer(d18:1(4E)) Identifier CHEBI:90307 Charge 0 Formula C65H112N3O37R SMILEShelp_outline [C@H]1(O[C@@H]([C@H](O)[C@@H]([C@H]1O)O[C@@H]2O[C@H](CO)[C@H]([C@@H]([C@H]2NC(=O)C)O)O[C@@H]3O[C@@H]([C@H](O)[C@@H]([C@H]3O)O)CO)CO)O[C@H]4[C@@H]([C@@H](NC(=O)C)[C@H](O[C@@H]5[C@H]([C@H](O[C@H]6[C@@H]([C@H]([C@H](OC[C@@H]([C@@H](/C=C/CCCCCCCCCCCCC)O)NC(*)=O)O[C@@H]6CO)O)O)O[C@@H]([C@@H]5O)CO)O)O[C@@H]4CO)O[C@@H]7O[C@H]([C@H]([C@H]([C@@H]7O)O)O)C 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline GDP Identifier CHEBI:58189 Charge -3 Formula C10H12N5O11P2 InChIKeyhelp_outline QGWNDRXFNXRZMB-UUOKFMHZSA-K SMILEShelp_outline Nc1nc2n(cnc2c(=O)[nH]1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 169 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:48336 | RHEA:48337 | RHEA:48338 | RHEA:48339 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
More general form(s) of this reaction
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RHEA:48364
β-D-Gal-(1→4)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-Glc-(1↔1ʼ)-Cer + GDP-β-L-fucose = β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-[α-L-fucosyl-(1→3)]-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1ʼ)-ceramide + GDP + H+
Publications
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Acceptor specificity of different length constructs of human recombinant alpha 1,3/4-fucosyltransferases. Replacement of the stem region and the transmembrane domain of fucosyltransferase V by protein A results in an enzyme with GDP-fucose hydrolyzing activity.
de Vries T., Srnka C.A., Palcic M.M., Swiedler S.J., van den Eijnden D.H., Macher B.A.
The acceptor specificity of recombinant full-length, membrane-bound fucosyltransferases, expressed in COS-7 cells, and soluble, protein-A chimeric forms of alpha 1,3-fucosyltransferase (Fuc-T) III, Fuc-TIV, and Fuc-TV was analyzed toward a broad panel of oligosaccharide, glycolipid, and glycoprote ... >> More
The acceptor specificity of recombinant full-length, membrane-bound fucosyltransferases, expressed in COS-7 cells, and soluble, protein-A chimeric forms of alpha 1,3-fucosyltransferase (Fuc-T) III, Fuc-TIV, and Fuc-TV was analyzed toward a broad panel of oligosaccharide, glycolipid, and glycoprotein substrates. Our results on the full-length enzymes confirm and extend previous studies. However, chimeric Fuc-Ts showed increased activity toward glycoproteins, whereas chimeric Fuc-TIII and Fuc-TV had a decreased activity with glycosphingolipids, compared to the full-length enzymes. Unexpectedly, chimeric Fuc-TV exhibited a GDP-fucose hydrolyzing activity. In substrates with multiple acceptor sites, the preferred site of fucosylation was identified. Fuc-TIII and Fuc-TV catalyzed fucose transfer exclusively to OH-3 of glucose in lacto-N-neotetraose and lacto-N-tetraose, respectively, as was demonstrated by 1H NMR spectroscopy. Thin layer chromatography immunostaining revealed that FucT-IV preferred the distal GlcNAc residue in nLc6Cer, whereas Fuc-TV preferred the proximal Gl-cNAc residue. Incubation of Fuc-TIV or Fuc-TV with VI3NeuAcnLc6Cer resulted in products with the sialyl-LewisX epitope as well as the VIM-2 structure. To identify polar groups on acceptors that function in enzyme binding, deoxygenated substrate analogs were tested as acceptors. All three Fuc-Ts had an absolute requirement for a hydroxyl at C-6 of galactose in addition to the accepting hydroxyl at C-3 or C-4 of GlcNAc. << Less
J. Biol. Chem. 270:8712-8722(1995) [PubMed] [EuropePMC]
This publication is cited by 16 other entries.