Enzymes
| UniProtKB help_outline | 229 proteins |
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- Name help_outline a neolactoside nLc4Cer Identifier CHEBI:90376 Charge 0 Formula C30H50N2O23R2 SMILEShelp_outline [C@H]([C@@H](*)O)(NC(=O)*)CO[C@@H]1O[C@@H]([C@@H](O[C@H]2[C@@H]([C@@H](O[C@H]3[C@@H]([C@H]([C@H](O[C@@H]4O[C@@H]([C@H](O)[C@@H]([C@H]4O)O)CO)[C@H](O3)CO)O)NC(C)=O)[C@H]([C@@H](CO)O2)O)O)[C@@H]([C@H]1O)O)CO 2D coordinates Mol file for the small molecule Search links Involved in 12 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 IV2-α-Fuc-nLc4Cer Identifier CHEBI:90803 Charge 0 Formula C36H60N2O27R2 SMILEShelp_outline O([C@H]1[C@@H]([C@@H](NC(C)=O)[C@H](O[C@@H]2[C@H]([C@H](O[C@H]3[C@@H]([C@H]([C@H](OC[C@@H]([C@@H](*)O)NC(*)=O)O[C@@H]3CO)O)O)O[C@@H]([C@@H]2O)CO)O)O[C@@H]1CO)O)[C@H]4[C@@H]([C@H]([C@H]([C@H](O4)CO)O)O)O[C@@H]5O[C@H]([C@H]([C@H]([C@@H]5O)O)O)C 2D coordinates Mol file for the small molecule Search links Involved in 6 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:48800 | RHEA:48801 | RHEA:48802 | RHEA:48803 | |
|---|---|---|---|---|
| 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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Characterization of three members of murine alpha1,2-fucosyltransferases: change in the expression of the Se gene in the intestine of mice after administration of microbes.
Lin B., Saito M., Sakakibara Y., Hayashi Y., Yanagisawa M., Iwamori M.
We cloned three members of a GDP-fucose:beta-galactoside alpha1,2-fucosyltransferase (alpha1,2-fucosyltransferase) family, MFUT-I, -II, and -III, from a cDNA of murine small intestine, and determined their enzymatic properties after transfection of the genes into COS-7 cells, and their expression ... >> More
We cloned three members of a GDP-fucose:beta-galactoside alpha1,2-fucosyltransferase (alpha1,2-fucosyltransferase) family, MFUT-I, -II, and -III, from a cDNA of murine small intestine, and determined their enzymatic properties after transfection of the genes into COS-7 cells, and their expression in murine tissues by Northern blotting. MFUT-I, -II, and -III exhibited sequence homology with the human H (78.4%), Se (79.0%), and Sec1 (74.9%) gene products, respectively. COS-7 cells transfected with MFUT-I and -II exhibited alpha1,2-fucosyltransferase activity and the best acceptor substrate for both gene products was GA1 to yield a fucosyl GA1 structure, but no activity was detected in COS-7 cells with MFUT-III. MFUT-II yielded a 3.5-kb mRNA transcript in several tissues, whereas MFUT-I and -III were predominantly expressed in epididymis and testis, respectively. The administration of microbes into germ-free mice resulted in a rapid increase of the MFUT-II gene (Se gene) for the synthesis of fucosyl GA1 in the intestine. << Less
Arch. Biochem. Biophys. 388:207-215(2001) [PubMed] [EuropePMC]
This publication is cited by 8 other entries.
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Tissue-specific loss of fucosylated glycolipids in mice with targeted deletion of alpha(1,2)fucosyltransferase genes.
Iwamori M., Domino S.E.
Glycolipids in epithelial tissues of the gastrointestinal tract act as receptors for enteric bacteria and are implicated in the activation of the intestinal immune system. To clarify the genes involved in the fucosylation of the major glycolipids, substrate glycolipids and fucosylated products wer ... >> More
Glycolipids in epithelial tissues of the gastrointestinal tract act as receptors for enteric bacteria and are implicated in the activation of the intestinal immune system. To clarify the genes involved in the fucosylation of the major glycolipids, substrate glycolipids and fucosylated products were measured in tissues of wild-type and mutant mice lacking alpha(1,2)fucosyltransferase genes FUT1 or FUT2. Quantitative determination was performed by TLC-immunostaining for GA1 (Gg4Cer), FGA1 (fucosyl GA1), GM1 (II3NeuAc-Gg4Cer), FGM1 (fucosyl GM1), and Forssman glycolipids. Both FGM1 and FGA1 completely disappeared from the antrum, cecum, and colon of FUT2-null mice, but not those of FUT1-null and wild-type mice. Precursor glycolipids, GM1 and GA1, accumulated in tissues of FUT2-null mice, indicating that the FUT2-encoded enzyme preferentially participates in the fucosylation of GA1 and GM1 in these tissues. Female reproductive organs were similarly found to utilize FUT2 for the fucosylation of glycolipids FGA1 (uterus and cervix), and FGM1 (ovary), due to their absence in FUT2-null mice. In FUT1-null mice FGA1 was lost from the pancreas, but was present in wild-type and FUT2-null mice, indicating that FUT1 is essential for fucosylation of GA1 in the pancreas. Ulex europaeus agglutinin-I lectin histochemistry for alpha(1,2)fucose residues confirmed the absence of alpha(1,2)fucose residues from the apical surface of pancreatic acinar glands of FUT1-null mice. Ileum, epididymis, and testis retained specific fucosylated glycolipids, irrespective of targeted deletion of either gene, indicating either compensation for or redundancy of the alpha(1,2)fucosyltransferase genes in these tissues. << Less
Biochem. J. 380:75-81(2004) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.