Enzymes
| UniProtKB help_outline | 1 proteins |
Reaction participants Show >> << Hide
- Name help_outline a ganglioside Fuc-GM1 Identifier CHEBI:90189 Charge -1 Formula C47H76N3O35R2 SMILEShelp_outline O1[C@H]([C@H]([C@H]([C@@H]([C@@H]1O[C@H]2[C@@H](O[C@@H]([C@@H]([C@@H]2O)O)CO)O[C@@H]3[C@H]([C@@H](O[C@@H]([C@@H]3O)CO)O[C@@H]4[C@@H]([C@H]([C@@H](O[C@@H]4CO)O[C@@H]5[C@H](O[C@@H](OC[C@@H]([C@@H](*)O)NC(*)=O)[C@@H]([C@H]5O)O)CO)O)O[C@@]6(C[C@@H]([C@H]([C@@](O6)([C@@H]([C@@H](CO)O)O)[H])NC(C)=O)O)C(=O)[O-])NC(C)=O)O)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 α-Fuc-(1→2)-β-Gal-(1→3)-β-GalNAc-(1→4)-[α-Neu5Ac-(2→3)]-β-Gal-(1→4)-Glc Identifier CHEBI:156538 Charge -1 Formula C43H71N2O33 InChIKeyhelp_outline HZUOSHNDAQUEQC-URPMETKKSA-M SMILEShelp_outline O1[C@H]([C@H]([C@H]([C@@H]([C@@H]1O[C@H]2[C@@H](O[C@@H]([C@@H]([C@@H]2O)O)CO)O[C@@H]3[C@H]([C@@H](O[C@@H]([C@@H]3O)CO)O[C@@H]4[C@@H]([C@H]([C@@H](O[C@@H]4CO)O[C@@H]5[C@H](OC(O)[C@@H]([C@H]5O)O)CO)O)O[C@@]6(C[C@@H]([C@H]([C@@](O6)([C@@H]([C@@H](CO)O)O)[H])NC(C)=O)O)C(=O)[O-])NC(C)=O)O)O)O)C 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 an N-acyl-sphingoid base Identifier CHEBI:83273 Charge 0 Formula C4H7NO3R2 SMILEShelp_outline OC[C@H](NC([*])=O)[C@H](O)[*] 2D coordinates Mol file for the small molecule Search links Involved in 263 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:65548 | RHEA:65549 | RHEA:65550 | RHEA:65551 | |
|---|---|---|---|---|
| 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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Structural Insights into the Broad Substrate Specificity of a Novel Endoglycoceramidase I Belonging to a New Subfamily of GH5 Glycosidases.
Han Y.B., Chen L.Q., Li Z., Tan Y.M., Feng Y., Yang G.Y.
Endoglycoceramidases (EGCases) specifically hydrolyze the glycosidic linkage between the oligosaccharide and the ceramide moieties of various glycosphingolipids, and they have received substantial attention in the emerging field of glycosphingolipidology. However, the mechanism regulating the stri ... >> More
Endoglycoceramidases (EGCases) specifically hydrolyze the glycosidic linkage between the oligosaccharide and the ceramide moieties of various glycosphingolipids, and they have received substantial attention in the emerging field of glycosphingolipidology. However, the mechanism regulating the strict substrate specificity of these GH5 glycosidases has not been identified. In this study, we report a novel EGCase I from <i>Rhodococcus equi</i> 103S (103S_EGCase I) with remarkably broad substrate specificity. Based on phylogenetic analyses, the enzyme may represent a new subfamily of GH5 glycosidases. The X-ray crystal structures of 103S_EGCase I alone and in complex with its substrates monosialodihexosylganglioside (GM3) and monosialotetrahexosylganglioside (GM1) enabled us to identify several structural features that may account for its broad specificity. Compared with EGCase II from <i>Rhodococcus</i> sp. M-777 (M777_EGCase II), which possesses strict substrate specificity, 103S_EGCase I possesses a longer α7-helix and a shorter loop 4, which forms a larger substrate-binding pocket that could accommodate more extended oligosaccharides. In addition, loop 2 and loop 8 of the enzyme adopt a more open conformation, which also enlarges the oligosaccharide-binding cavity. Based on this knowledge, a rationally designed experiment was performed to examine the substrate specificity of EGCase II. The truncation of loop 4 in M777_EGCase II increased its activity toward GM1 (163%). Remarkably, the S63G mutant of M777_EGCase II showed a broader substrate spectra and significantly increased activity toward bulky substrates (up to >1370-fold for fucosyl-GM1). Collectively, the results presented here reveal the exquisite substrate recognition mechanism of EGCases and provide an opportunity for further engineering of these enzymes. << Less
J. Biol. Chem. 292:4789-4800(2017) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.