Reaction participants Show >> << Hide
- Name help_outline a neolactoside IV3-α-NeuAc-nLc4Cer(d18:1(4E)) Identifier CHEBI:58665 Charge -1 Formula C56H95N3O31R SMILEShelp_outline [H][C@]1(O[C@@](C[C@H](O)[C@H]1NC(C)=O)(O[C@H]1[C@@H](O)[C@@H](CO)O[C@@H](O[C@H]2[C@H](O)[C@@H](NC(C)=O)[C@@H](O[C@@H]2CO)O[C@H]2[C@@H](O)[C@@H](CO)O[C@@H](O[C@H]3[C@H](O)[C@@H](O)[C@H](OC[C@H](NC([*])=O)[C@H](O)\C=C\CCCCCCCCCCCCC)O[C@@H]3CO)[C@@H]2O)[C@@H]1O)C([O-])=O)[C@H](O)[C@H](O)CO 2D coordinates Mol file for the small molecule Search links Involved in 3 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 IV3-α-NeuNAc,III3-α-Fuc-nLc4Cer(d18:1(4E)) Identifier CHEBI:144418 Charge -1 Formula C62H105N3O35R SMILEShelp_outline [C@H]1(O[C@@H]([C@@H]([C@@H]([C@H]1O)O[C@]2(O[C@]([C@@H]([C@H](C2)O)NC(C)=O)([C@@H]([C@@H](CO)O)O)[H])C([O-])=O)O)CO)O[C@H]3[C@@H]([C@H]([C@@H](O[C@@H]3CO)O[C@@H]4[C@H]([C@@H](O[C@@H]([C@@H]4O)CO)O[C@H]5[C@@H]([C@H]([C@@H](O[C@@H]5CO)OC[C@@H]([C@@H](/C=C/CCCCCCCCCCCCC)O)NC(=O)*)O)O)O)NC(=O)C)O[C@@H]6O[C@H]([C@H]([C@H]([C@@H]6O)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:77715 | RHEA:77716 | RHEA:77717 | RHEA:77718 | |
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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
Publications
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Fucosylation of complex glycosphingolipids by recombinant fucosyltransferase-VII.
Stroud M.R., Holmes E.H.
Fucosyltransferase VII (FucT-VII) is one of five known alpha 1-->3fucosyltransferases capable of transferring fucose to the C-3 position of N-acetylglucosamine residues found in lactosamine based glycans. Previous studies have indicated that FucT-VII has a very restricted specificity, capable of f ... >> More
Fucosyltransferase VII (FucT-VII) is one of five known alpha 1-->3fucosyltransferases capable of transferring fucose to the C-3 position of N-acetylglucosamine residues found in lactosamine based glycans. Previous studies have indicated that FucT-VII has a very restricted specificity, capable of fucosylating only terminally alpha 2-->3sialylated carbohydrate substrates, resulting in the synthesis of the sialyl Lewis x (sLe(x)) epitope. Although FucT-VII is expressed in cells of myeloid origin, the monosialylganglioside fraction of HL60 cells contains only internally and/or multiply fucosylated polylactosamine structures; no monofucosylated sLe(x) derivatives are detected. We now report that the structure of the final product formed by the action of FucT-VII on sialynorhexaosylceramide (a glycosphingolipid substrate having multiple fucosylation sites) is extended monofucosyl sLe(x) and fucosylation is restricted to the terminal GlcNAc-V. This indicates that the biosynthesis of all fucosylated monosialylated gangliosides found in HL60 cells (including the E-selectin binding fractions) involves at least one additional alpha 1-->3fucosyltransferase. << Less
Biochem. Biophys. Res. Commun. 238:165-168(1997) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.