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- Name help_outline 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 Identifier CHEBI:90357 Charge 0 Formula C44H73N3O33R2 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](*)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 5 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 β-D-Gal-(1→4)-[α-L-Fuc-(1→3)]-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 Identifier CHEBI:90360 Charge 0 Formula C50H83N3O37R2 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[C@@H]3O[C@H]([C@H]([C@H]([C@@H]3O)O)O)C)O[C@@H]4O[C@@H]([C@H](O)[C@@H]([C@H]4O)O)CO)CO)O[C@H]5[C@@H]([C@@H](NC(C)=O)[C@H](O[C@@H]6[C@H]([C@H](O[C@H]7[C@@H]([C@H]([C@H](OC[C@@H]([C@@H](*)O)NC(*)=O)O[C@@H]7CO)O)O)O[C@@H]([C@@H]6O)CO)O)O[C@@H]5CO)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 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:48368 | RHEA:48369 | RHEA:48370 | RHEA:48371 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
Specific form(s) of this reaction
Publications
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Site-specific fucosylation of sialylated polylactosamines by alpha1,3/4-fucosyltransferases-V and -VI Is defined by amino acids near the N terminus of the catalytic domain.
Shetterly S., Jost F., Watson S.R., Knegtel R., Macher B.A., Holmes E.H.
Fucose transfer from GDP-fucose to GlcNAc residues of the sialylated polylactosamine acceptor NeuAcalpha2-3Galbeta1-4Glc-NAcbeta1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glcbeta1-ceramide leads to two isomeric monofucosyl antigens, VIM2 and sialyl-Le(x). Human alpha1,3/4-fucosyltransferase (FucT)-V cata ... >> More
Fucose transfer from GDP-fucose to GlcNAc residues of the sialylated polylactosamine acceptor NeuAcalpha2-3Galbeta1-4Glc-NAcbeta1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glcbeta1-ceramide leads to two isomeric monofucosyl antigens, VIM2 and sialyl-Le(x). Human alpha1,3/4-fucosyltransferase (FucT)-V catalyzes primarily the synthesis of VIM2, whereas human FucT-VI catalyzes primarily the synthesis of sialyl-Le(x). Thus, these two enzymes have distinct "site-specific fucosylation" properties. Amino acid sequence alignment of these enzymes showed that there are 24 amino acid differences in their catalytic domains. Studies were conducted to determine which of the amino acid differences are responsible for the site-specific fucosylation properties of each enzyme. Domain swapping (replacing a portion of the catalytic domain from one enzyme with an analogous portion from the other enzyme) demonstrated that site-specific fucosylation was defined within a 40-amino acid segment containing 8 amino acid differences between the two enzymes. Site-directed mutagenesis studies demonstrated that the site-specific fucosylation properties of these enzymes could be reversed by substituting 4 amino acids from one sequence with the other. These results were observed in both in vitro enzyme assays and flow cytometric analyses of Chinese hamster ovary cells transfected with plasmids containing the various enzyme constructs. Modeling studies of human FucT using a structure of a bacterial fucosyltransferase as a template demonstrated that the amino acids responsible for site-specific fucosylation map near the GDP-fucose-binding site. Additional enzyme studies demonstrated that FucT-VI has approximately 12-fold higher activity compared with FucT-V and that the Trp(124)/Arg(110) site in these enzymes is responsible primarily for this activity difference. << Less
J. Biol. Chem. 282:24882-24892(2007) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.