Enzymes
| UniProtKB help_outline | 1,513 proteins |
Reaction participants Show >> << Hide
- Name help_outline α-D-galactosyl-(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:90380 Charge 0 Formula C36H60N2O28R2 SMILEShelp_outline [C@H]1(O[C@@H]([C@@H]([C@@H]([C@H]1O)O[C@@H]2[C@@H]([C@H]([C@H]([C@H](O2)CO)O)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](*)O)NC(=O)*)O)O)O)NC(=O)C)O 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-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-Gal,III3-α-Fuc-nLc4Cer Identifier CHEBI:90381 Charge 0 Formula C42H70N2O32R2 SMILEShelp_outline C[C@@H]1O[C@@H](O[C@@H]2[C@@H](NC(C)=O)[C@H](O[C@H]3[C@@H](O)[C@@H](CO)O[C@@H](O[C@H]4[C@H](O)[C@@H](O)[C@H](OC[C@H](NC([*])=O)[C@H](O)[*])O[C@@H]4CO)[C@@H]3O)O[C@H](CO)[C@H]2O[C@@H]2O[C@H](CO)[C@H](O)[C@H](O[C@H]3O[C@H](CO)[C@H](O)[C@H](O)[C@H]3O)[C@H]2O)[C@@H](O)[C@H](O)[C@@H]1O 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:48380 | RHEA:48381 | RHEA:48382 | RHEA:48383 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
Publications
-
Alpha1,3-fucosyltransferase IX (Fut9) determines Lewis X expression in brain.
Nishihara S., Iwasaki H., Nakajima K., Togayachi A., Ikehara Y., Kudo T., Kushi Y., Furuya A., Shitara K., Narimatsu H.
The expression of the Lewis X (Lex) carbohydrate structure in brain is developmentally regulated and is thought to play a role in cell-cell interaction during neuronal development. Mice possess three functional alpha1,3-fucosyltransferase genes: Fut4, Fut7, and Fut9. Fut7 is known to have no activ ... >> More
The expression of the Lewis X (Lex) carbohydrate structure in brain is developmentally regulated and is thought to play a role in cell-cell interaction during neuronal development. Mice possess three functional alpha1,3-fucosyltransferase genes: Fut4, Fut7, and Fut9. Fut7 is known to have no activity to synthesize Lex. In the present study, the relative activities of Fut4 and Fut9 for Lex synthesis were determined using recombinant enzymes. Fut9 exhibited very strong activity for oligosaccharide acceptors and glycolipid acceptors, that is, more than 10- and 100-fold, respectively, than that of Fut4. Furthermore, both cerebrum and cerebellum at various stages of development (E17, P0, P7, P30, P100) expressed 15-100 times more Fut9 transcript than Fut4 transcript. Neurons and astrocytes in primary culture also expressed 10-15 times more Fut9 than Fut4 transcript. Moreover, alpha1,3-Fut activity toward a polylactosamine chain in homogenates of brain tissues and primary cultured cells showed a pattern typical of Fut9, not Fut4. The developmental profile of activity for the synthesis of Lex was well correlated with that of Fut9 transcript. Immunohistochemistry with anti-Fut9 monoclonal antibody revealed the distribution of the Lex structure. These results showed that Fut9 is the most responsible enzyme for the synthesis of Lex in brain. << Less
Glycobiology 13:445-455(2003) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.