Enzymes
| UniProtKB help_outline | 1,944 proteins |
| Enzyme class help_outline |
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Reaction participants Show >> << Hide
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Namehelp_outline
3-O-(α-L-fucosyl)-L-threonyl-[EGF-like domain protein]
Identifier
RHEA-COMP:17923
Reactive part
help_outline
- Name help_outline 3-O-(α-L-fucosyl)-L-threonyl residue Identifier CHEBI:189631 Charge 0 Formula C10H17NO6 SMILEShelp_outline O[C@@H]1[C@@H]([C@@H](O[C@H]([C@H]1O)O[C@@H]([C@@H](C(*)=O)N*)C)C)O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline UDP-N-acetyl-α-D-glucosamine Identifier CHEBI:57705 (Beilstein: 4286654) help_outline Charge -2 Formula C17H25N3O17P2 InChIKeyhelp_outline LFTYTUAZOPRMMI-CFRASDGPSA-L SMILEShelp_outline CC(=O)N[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1OP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 88 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
3-O-(N-acetyl-β-D-glucosaminyl-(1→3)-α-L-fucosyl)-L-threonyl-[EGF-like domain protein]
Identifier
RHEA-COMP:17922
Reactive part
help_outline
- Name help_outline 3-O-(N-acetyl-β-D-glucosaminyl-(1→3)-α-L-fucosyl)-L-threonyl residue Identifier CHEBI:189634 Charge 0 Formula C18H30N2O11 SMILEShelp_outline O([C@@H]1[C@@H]([C@@H](O[C@H]([C@H]1O)O[C@@H]([C@@H](C(*)=O)N*)C)C)O)[C@@H]2O[C@@H]([C@H]([C@@H]([C@H]2NC(=O)C)O)O)CO 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 UDP Identifier CHEBI:58223 Charge -3 Formula C9H11N2O12P2 InChIKeyhelp_outline XCCTYIAWTASOJW-XVFCMESISA-K SMILEShelp_outline O[C@@H]1[C@@H](COP([O-])(=O)OP([O-])([O-])=O)O[C@H]([C@@H]1O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 577 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 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:70531 | RHEA:70532 | RHEA:70533 | RHEA:70534 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Fringe is a glycosyltransferase that modifies Notch.
Moloney D.J., Panin V.M., Johnston S.H., Chen J., Shao L., Wilson R., Wang Y., Stanley P., Irvine K.D., Haltiwanger R.S., Vogt T.F.
Notch receptors function in highly conserved intercellular signalling pathways that direct cell-fate decisions, proliferation and apoptosis in metazoans. Fringe proteins can positively and negatively modulate the ability of Notch ligands to activate the Notch receptor. Here we establish the bioche ... >> More
Notch receptors function in highly conserved intercellular signalling pathways that direct cell-fate decisions, proliferation and apoptosis in metazoans. Fringe proteins can positively and negatively modulate the ability of Notch ligands to activate the Notch receptor. Here we establish the biochemical mechanism of Fringe action. Drosophila and mammalian Fringe proteins possess a fucose-specific beta1,3 N-acetylglucosaminyltransferase activity that initiates elongation of O-linked fucose residues attached to epidermal growth factor-like sequence repeats of Notch. We obtained biological evidence that Fringe-dependent elongation of O-linked fucose on Notch modulates Notch signalling by using co-culture assays in mammalian cells and by expression of an enzymatically inactive Fringe mutant in Drosophila. The post-translational modification of Notch by Fringe represents a striking example of modulation of a signalling event by differential receptor glycosylation and identifies a mechanism that is likely to be relevant to other signalling pathways. << Less
Nature 406:369-375(2000) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Glycosyltransferase activity of Fringe modulates Notch-Delta interactions.
Bruckner K., Perez L., Clausen H., Cohen S.
Ligands that are capable of activating Notch family receptors are broadly expressed in animal development, but their activity is tightly regulated to allow formation of tissue boundaries. Members of the fringe gene family have been implicated in limiting Notch activation during boundary formation, ... >> More
Ligands that are capable of activating Notch family receptors are broadly expressed in animal development, but their activity is tightly regulated to allow formation of tissue boundaries. Members of the fringe gene family have been implicated in limiting Notch activation during boundary formation, but the mechanism of Fringe function has not been determined. Here we present evidence that Fringe acts in the Golgi as a glycosyltransferase enzyme that modifies the epidermal growth factor (EGF) modules of Notch and alters the ability of Notch to bind its ligand Delta. Fringe catalyses the addition of N-acetylglucosamine to fucose, which is consistent with a role in the elongation of O-linked fucose O-glycosylation that is associated with EGF repeats. We suggest that cell-type-specific modification of glycosylation may provide a general mechanism to regulate ligand-receptor interactions in vivo. << Less
Nature 406:411-415(2000) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.