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Namehelp_outline
a 3-O-[β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl]-L-seryl-[protein]
Identifier
RHEA-COMP:13922
Reactive part
help_outline
- Name help_outline a 3-O-[β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl]-L-serine residue Identifier CHEBI:137949 Charge 0 Formula C17H28N2O12 SMILEShelp_outline [C@H]1([C@@H]([C@H]([C@H]([C@H](O1)CO)O)O[C@H]2[C@@H]([C@H]([C@H]([C@H](O2)CO)O)O)O)NC(=O)C)OC[C@@H](C(=O)*)N* 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CMP-N-acetyl-β-neuraminate Identifier CHEBI:57812 (Beilstein: 5899715) help_outline Charge -2 Formula C20H29N4O16P InChIKeyhelp_outline TXCIAUNLDRJGJZ-BILDWYJOSA-L SMILEShelp_outline [H][C@]1(O[C@](C[C@H](O)[C@H]1NC(C)=O)(OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1ccc(N)nc1=O)C([O-])=O)[C@H](O)[C@H](O)CO 2D coordinates Mol file for the small molecule Search links Involved in 91 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
a 3-O-{β-D-galactosyl-(1→3)-[N-acetyl-α-neuraminosyl-(2→6)]-N-acetyl-α-D-galactosaminyl}-L-seryl-[protein]
Identifier
RHEA-COMP:19724
Reactive part
help_outline
- Name help_outline a 3-O-{β-D-galactosyl-(1→3)-[N-acetyl-α-neuraminosyl-(2→6)]-N-acetyl-α-D-galactosaminyl}-L-serine residue Identifier CHEBI:231973 Charge -1 Formula C28H44N3O20 SMILEShelp_outline [H][C@]1(O[C@@](C[C@H](O)[C@H]1NC(C)=O)(OC[C@H]1O[C@H](OC[C@H](N-*)C(-*)=O)[C@H](NC(C)=O)[C@@H](O[C@@H]2O[C@H](CO)[C@H](O)[C@H](O)[C@H]2O)[C@H]1O)C([O-])=O)[C@H](O)[C@H](O)CO 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 CMP Identifier CHEBI:60377 Charge -2 Formula C9H12N3O8P InChIKeyhelp_outline IERHLVCPSMICTF-XVFCMESISA-L SMILEShelp_outline Nc1ccn([C@@H]2O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@H]2O)c(=O)n1 2D coordinates Mol file for the small molecule Search links Involved in 173 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 9,717 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:81655 | RHEA:81656 | RHEA:81657 | RHEA:81658 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Products of Chemoenzymatic Synthesis Representing MUC1 Tandem Repeat Unit with T-, ST- or STn-antigen Revealed Distinct Specificities of Anti-MUC1 Antibodies.
Yoshimura Y., Denda-Nagai K., Takahashi Y., Nagashima I., Shimizu H., Kishimoto T., Noji M., Shichino S., Chiba Y., Irimura T.
Anti-mucin1 (MUC1) antibodies have long been used clinically in cancer diagnosis and therapy and specific bindings of some of them are known to be dependent on the differential glycosylation of MUC1. However, a systematic comparison of the binding specificities of anti-MUC1 antibodies was not prev ... >> More
Anti-mucin1 (MUC1) antibodies have long been used clinically in cancer diagnosis and therapy and specific bindings of some of them are known to be dependent on the differential glycosylation of MUC1. However, a systematic comparison of the binding specificities of anti-MUC1 antibodies was not previously conducted. Here, a total of 20 glycopeptides including the tandem repeat unit of MUC1, APPAHGVTSAPDTRPAPGSTAPPAHGV with GalNAc (Tn-antigen), Galβ1-3GalNAc (T-antigen), NeuAcα2-3Galβ1-3GalNAc (sialyl-T-antigen), or NeuAcα2-6GalNAc (sialyl-Tn-antigen) at each threonine or serine residue were prepared by a combination of chemical glycopeptide synthesis and enzymatic extension of carbohydrate chains. These glycopeptides were tested by the enzyme-linked immunosorbent assay (ELISA) for their capacity to bind 13 monoclonal antibodies (mAbs) known to be specific for MUC1. The results indicated that anti-MUC1 mAbs have diverse specificities but can be classified into a few characteristic groups based on their binding pattern toward glycopeptides in some cases having a specific glycan at unique glycosylation sites. Because the clinical significance of some of these antibodies was already established, the structural features identified by these antibodies as revealed in the present study should provide useful information relevant to their further clinical use and the biological understanding of MUC1. << Less
Sci Rep 9:16641-16641(2019) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.