Enzymes
| UniProtKB help_outline | 8 proteins |
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- 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 N-acetyl-α-neuraminosyl-(2→3)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1ʼ)-ceramide Identifier CHEBI:90339 Charge -1 Formula C55H89N4O41R2 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)O[C@@H]6[C@H]([C@@H](O[C@@H]([C@@H]6O)CO)O[C@H]7[C@@H]([C@H]([C@@H](O[C@@H]7CO)OC[C@@H]([C@@H](*)O)NC(=O)*)O)O)O)NC(C)=O)O)O)NC(=O)C)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
- Name help_outline N-acetyl-α-neuraminosyl-(2→3)-β-D-galactosyl-(1→4)-[α-L-fucosyl-(1→3)]-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1ʼ)-ceramide Identifier CHEBI:90336 Charge -1 Formula C61H99N4O45R2 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)O[C@@H]6[C@H]([C@@H](O[C@@H]([C@@H]6O)CO)O[C@H]7[C@@H]([C@H]([C@@H](O[C@@H]7CO)OC[C@@H]([C@@H](*)O)NC(=O)*)O)O)O)NC(C)=O)O)O)NC(=O)C)O[C@@H]8O[C@H]([C@H]([C@H]([C@@H]8O)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
Cross-references
| RHEA:48356 | RHEA:48357 | RHEA:48358 | RHEA:48359 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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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.
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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.