Enzymes
| UniProtKB help_outline | 3,326 proteins |
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Namehelp_outline
an N4-(oligosaccharide-(1→3)-[oligosaccharide-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc)-L-asparaginyl-[protein]
Identifier
RHEA-COMP:18176
Reactive part
help_outline
- Name help_outline an N4-(oligosaccharide-(1→3)-[oligosaccharide-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc)-L-asparaginyl residue Identifier CHEBI:192714 Charge 0 Formula C26H40N4O17R2 SMILEShelp_outline N([C@@H]1O[C@@H]([C@H]([C@@H]([C@H]1NC(=O)C)O)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*)O)O)NC(C)=O)CO)C(C[C@@H](C(*)=O)N*)=O 2D coordinates Mol file for the small molecule Search links Involved in 10 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (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 6,264 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline an oligosaccharide-(1→3)-[oligosaccharide-(1→6)]-β-D-Man-(1→4)-D-GlcNAc Identifier CHEBI:192715 Charge 0 Formula C14H23NO11R2 SMILEShelp_outline OC1[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)O*)O)O)NC(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
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Namehelp_outline
N4-(N-acetyl-β-D-glucosaminyl)-L-asparaginyl-[protein]
Identifier
RHEA-COMP:12603
Reactive part
help_outline
- Name help_outline N4-(N-acetyl-β-D-glucosyl)-L-asparagine residue Identifier CHEBI:132248 Charge 0 Formula C12H19N3O7 SMILEShelp_outline C([C@@H](C(*)=O)N*)C(N[C@H]1[C@@H]([C@H]([C@@H]([C@H](O1)CO)O)O)NC(C)=O)=O 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
Cross-references
| RHEA:73067 | RHEA:73068 | RHEA:73069 | RHEA:73070 | |
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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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Demonstration and cytosolic location of an endo-N-acetyl-beta-D-glucosaminidase activity towards an asialo-N-acetyl-lactosaminic-type substrate in rat liver.
Pierce R.J., Spik G., Montreuil J.
An endo-N-acetyl-beta-D-glucosaminidase activity towards an asialo-N-acetyl-lactosaminic-type glycoasparagine substrate was demonstrated in rat liver. This activity was optimal at pH 7.0 and was predominantly present in the soluble (cytosolic) fraction.
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The release of intact oligosaccharides from specific glycoproteins by endo-beta-N-acetylglucosaminidase H.
Tarentino A.L., Plummer T.H. Jr., Maley F.
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Structural studies of two ovalbumin glycopeptides in relation to the endo-beta-N-acetylglucosaminidase specificity.
Tai T., Yamashita K., Ogata-Arakawa M., Koide N., Muramatsu T., Iwashita S., Inoue Y., Kobata A.
Heterogeneities of the two ovalbumin glycopeptides, (Man)5(GlcNAc)2Asn and (Man)6(GlcNAc)2Asn, were revealed by borate paper electrophoresis of oligosaccharide alcohols obtained from the glycopeptides by endo-beta-N-acetylglucosaminidase H digestion and NaB3H4 reduction. The structures of the majo ... >> More
Heterogeneities of the two ovalbumin glycopeptides, (Man)5(GlcNAc)2Asn and (Man)6(GlcNAc)2Asn, were revealed by borate paper electrophoresis of oligosaccharide alcohols obtained from the glycopeptides by endo-beta-N-acetylglucosaminidase H digestion and NaB3H4 reduction. The structures of the major components of the oligosaccharides were determined by the combination of methylation analysis, acetolysis, and alpha-mannosidase digestion. Based on the results, the whole structures of the major components of (Man)5(GlcNAc)2Asn and (Man)6(GlcNAc)2Asn were elucidated as Manalpha1 leads to 6[Manalpha1 leads to 3]-Manalpha1 leads to 6[Manalpha1 leads to 3[Manbeta1 leads to 4GlcNAcbeta1 leads to 4GlcNAc leads to Asn and Manalpha1 leads to 6[Manalpha1 leads to 3]Manalpha1 leads to 6[Manalpha1 leads to 2Manalpha1 leads to 3]Manbeta1 leads to 4GlcNAcbeta1 leads to GlcNAc leads to Asn, respectively. Since endo-beta-N-acetylglucosamini dase D hydrolyzes (Man)5(GlcNAc)2Asn but not (Man)6(GlcNAc)2Asn, the presence of the unsubstituted alpha-mannosyl residue linked at the C-3 position of the terminal mannose of Manbeta1 leads to 4GlcNAcbeta1 leads to 4 GlcNAcAsn core must be essential for the action of the enzyme. << Less
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Endo-beta-N-acetylglucosaminidase acting on carbohydrate moieties of glycoproteins. Purification and properties of the enzyme from Diplococcus pneumoniae.
Koide N., Muramatsu T.
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Cytosolic location of an endo-N-acetyl-beta-D-glucosaminidase activity in rat liver and kidney.
Pierce R.J., Spik G., Montreuil J.
Endo-N-acetyl-beta-D-glucosaminidase activity towards an oligomannosidic type glycoamino acid substrate was found in the soluble fraction of rat liver and kidney. No evidence for a lysosomal form of the activity was found.
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Endo-beta-N-acetylglucosaminidase from fig latex.
Chien S., Weinburg R., Li S., Li Y.
Biochem Biophys Res Commun 76:317-323(1976) [PubMed] [EuropePMC]