Enzymes
UniProtKB help_outline | 6 proteins |
Reaction participants Show >> << Hide
- Name help_outline a ganglioside GD1a (d18:1(4E)) Identifier CHEBI:78445 Charge -2 Formula C67H111N4O39R SMILEShelp_outline CCCCCCCCCCCCC\C=C\[C@@H](O)[C@H](CO[C@@H]1O[C@H](CO)[C@@H](O[C@@H]2O[C@H](CO)[C@H](O[C@@H]3O[C@H](CO)[C@H](O)[C@H](O[C@@H]4O[C@H](CO)[C@H](O)[C@H](O[C@@]5(C[C@H](O)[C@@H](NC(C)=O)[C@@H](O5)[C@H](O)[C@H](O)CO)C([O-])=O)[C@H]4O)[C@H]3NC(C)=O)[C@H](O[C@@]3(C[C@H](O)[C@@H](NC(C)=O)[C@@H](O3)[C@H](O)[C@H](O)CO)C([O-])=O)[C@H]2O)[C@H](O)[C@H]1O)NC([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a ganglioside GM1 (d18:1(4E)) Identifier CHEBI:77709 Charge -1 Formula C56H95N3O31R SMILEShelp_outline C([C@@H]([C@@H](/C=C/CCCCCCCCCCCCC)O)NC(*)=O)O[C@H]1[C@@H]([C@H]([C@@H]([C@H](O1)CO)O[C@H]2[C@@H]([C@H]([C@H]([C@H](O2)CO)O[C@H]3[C@@H]([C@H]([C@H]([C@H](O3)CO)O)O[C@H]4[C@@H]([C@H]([C@H]([C@H](O4)CO)O)O)O)NC(C)=O)O[C@@]5(C[C@@H]([C@H]([C@@](O5)([C@@H]([C@@H](CO)O)O)[H])NC(C)=O)O)C([O-])=O)O)O)O 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N-acetylneuraminate Identifier CHEBI:35418 Charge -1 Formula C11H18NO9 InChIKeyhelp_outline SQVRNKJHWKZAKO-LUWBGTNYSA-M SMILEShelp_outline [H][C@]1(OC(O)(C[C@H](O)[C@H]1NC(C)=O)C([O-])=O)[C@H](O)[C@H](O)CO 2D coordinates Mol file for the small molecule Search links Involved in 38 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:47856 | RHEA:47857 | RHEA:47858 | RHEA:47859 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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The plasma membrane-associated sialidase MmNEU3 modifies the ganglioside pattern of adjacent cells supporting its involvement in cell-to-cell interactions.
Papini N., Anastasia L., Tringali C., Croci G., Bresciani R., Yamaguchi K., Miyagi T., Preti A., Prinetti A., Prioni S., Sonnino S., Tettamanti G., Venerando B., Monti E.
We describe herein the enzyme behavior of MmNEU3, the plasma membrane-associated sialidase from mouse (Mus musculus). MmNEU3 is localized at the plasma membrane as demonstrated directly by confocal microscopy analysis. In addition, administration of the radiolabeled ganglioside GD1a to MmNEU3-tran ... >> More
We describe herein the enzyme behavior of MmNEU3, the plasma membrane-associated sialidase from mouse (Mus musculus). MmNEU3 is localized at the plasma membrane as demonstrated directly by confocal microscopy analysis. In addition, administration of the radiolabeled ganglioside GD1a to MmNEU3-transfected cells, under conditions that prevent lysosomal activity, led to its hydrolysis into ganglioside GM1, further indicating the plasma membrane topology of MmNEU3. Metabolic labeling with [1-(3)H]sphingosine allowed the characterization of the ganglioside patterns of COS-7 cells. MmNEU3 expression in COS-7 cells led to an extensive modification of the cell ganglioside pattern, i.e. GM3 and GD1a content was decreased to about one-third compared with mock-transfected cells. At the same time, a 35% increase in ganglioside GM1 content was observed. Mixed culture of MmNEU3-transfected cells with [1-(3)H]sphingosine-labeled cells demonstrates that the enzyme present at the cell surface is able to recognize gangliosides exposed on the membrane of nearby cells. Under these experimental conditions, the extent of ganglioside pattern changes was a function of MmNEU3 transient expression. Overall, the variations in GM3, GD1a, and GM1 content were very similar to those observed in the case of [1-(3)H]sphingosine-labeled MmNEU3-transfected cells, indicating that the enzyme mainly exerted its activity toward ganglioside substrates present at the surface of neighboring cells. These results indicate that the plasma membrane-associated sialidase MmNEU3 is able to hydrolyze ganglioside substrates in intact living cells at a neutral pH, mainly through cell-to-cell interactions. << Less