Enzymes
| UniProtKB help_outline | 1,779 proteins |
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- Name help_outline a neolactoside IV2-α-Fuc-nLc4Cer(d18:1(4E)) Identifier CHEBI:28691 Charge 0 Formula C51H89N2O27R 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](/C=C/CCCCCCCCCCCCC)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 3 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 neolactoside nLc4Cer(d18:1(4E)) Identifier CHEBI:17006 Charge 0 Formula C45H79N2O23R 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](O[C@@H]3O[C@H](CO)[C@@H](O[C@@H]4O[C@H](CO)[C@H](O)[C@H](O)[C@H]4O)[C@H](O)[C@H]3NC(C)=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 L-fucose Identifier CHEBI:2181 (Beilstein: 1905878; CAS: 2438-80-4) help_outline Charge 0 Formula C6H12O5 InChIKeyhelp_outline SHZGCJCMOBCMKK-DHVFOXMCSA-N SMILEShelp_outline C[C@@H]1OC(O)[C@@H](O)[C@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 11 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:48224 | RHEA:48225 | RHEA:48226 | RHEA:48227 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Degradation of blood group A glycolipid A-6-2 by normal and mutant human skin fibroblasts.
Asfaw B., Schindler D., Ledvinova J., Cerny B., Smid F., Conzelmann E.
The degradation of blood group glycolipid A-6-2 (GalNAc(alpha1-->3)[Fuc alpha1-->2]Gal(beta1-->4)GlcNAc(beta1-->3)Gal(beta1-->4)Glc(beta1-->1')C er, IV2-alpha-fucosyl-IV3-alpha-N-acetylgalactosaminylneolact otetraosylceramide), tritium-labeled in its ceramide moiety, was studied in situ, in skin f ... >> More
The degradation of blood group glycolipid A-6-2 (GalNAc(alpha1-->3)[Fuc alpha1-->2]Gal(beta1-->4)GlcNAc(beta1-->3)Gal(beta1-->4)Glc(beta1-->1')C er, IV2-alpha-fucosyl-IV3-alpha-N-acetylgalactosaminylneolact otetraosylceramide), tritium-labeled in its ceramide moiety, was studied in situ, in skin fibroblast cultures from normal controls, from patients with defects of lysosomal alpha-N-acetylgalactosaminidase, and from patients with other lysosomal storage diseases. Uptake of the glycolipid with apolipoprotein E-coated liposomes was linear with time and with the amount of glycolipid added. In normal cells, the expected array of less polar products and some lipids resulting from re-using the liberated sphingosine, mainly sphingomyelin and phosphatidylcholine, were formed. In alpha-N-acetylgalactosaminidase-deficient cells, the glycolipid was virtually not degraded; product formation was less than 2% of the normal control rate, suggesting that blood group A-active glycolipids contribute as storage compounds to the pathogenesis of this disease. The expected accumulation of degradation intermediates was seen in fucosidosis, and in Sandhoff, Gaucher, and Farber disease cells, whereas normal turnover rates were found in Tay-Sachs disease cells, G(M2) activator-deficient (variant AB of G(M2) gangliosidosis) and in sulfatide activator-(sap-B-) deficient cells. In G(M1) gangliosidosis and in sap precursor-deficient cells, the lysosomal glycolipid catabolism was found to be strongly retarded; accumulation of individual products could not be seen. Skin fibroblasts from patients with alpha-N-acetylgalactosaminidase deficiency (Schindler disease) cannot degrade the major blood group A glycolipid. << Less
J. Lipid Res. 39:1768-1780(1998) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.