Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline an α-L-Fuc-(1→2)-β-D-Gal-(1→3)-β-D-GlcNAc derivative Identifier CHEBI:133509 Charge 0 Formula C20H34NO15R SMILEShelp_outline O[C@H]1[C@@H]([C@H]([C@@H](O[C@@H]1CO)O*)NC(C)=O)O[C@@H]2O[C@@H]([C@H](O)[C@H](O)[C@H]2O[C@@H]3O[C@H]([C@H]([C@H]([C@@H]3O)O)O)C)CO 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline UDP-N-acetyl-α-D-galactosamine Identifier CHEBI:67138 Charge -2 Formula C17H25N3O17P2 InChIKeyhelp_outline LFTYTUAZOPRMMI-NESSUJCYSA-L SMILEShelp_outline CC(=O)N[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1OP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 61 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline an α-D-GalNAc-(1→3)-[α-L-Fuc-(1→2)]-β-D-Gal-(1→3)-β-D-GlcNAc derivative Identifier CHEBI:233961 Charge 0 Formula C28H47N2O20R SMILEShelp_outline *OC1OC(CO)C(O)C(OC2OC(CO)C(O)C(OC3OC(CO)C(O)C(O)C3NC(=O)C)C2OC4OC(C)C(O)C(O)C4O)C1NC(=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 UDP Identifier CHEBI:58223 Charge -3 Formula C9H11N2O12P2 InChIKeyhelp_outline XCCTYIAWTASOJW-XVFCMESISA-K SMILEShelp_outline O[C@@H]1[C@@H](COP([O-])(=O)OP([O-])([O-])=O)O[C@H]([C@@H]1O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 711 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 10,232 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:84499 | RHEA:84500 | RHEA:84501 | RHEA:84502 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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| MetaCyc help_outline |
Related reactions help_outline
More general form(s) of this reaction
Publications
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Bacterial homologue of human blood group A transferase.
Yi W., Shen J., Zhou G., Li J., Wang P.G.
A bacterial version of human blood group A transferase was identified and found to be able to accept five naturally existing H-antigen core structures as good substrates, demonstrating its versatility for synthesis of blood group A antigens. Furthermore, this enzyme was applied in the engineering ... >> More
A bacterial version of human blood group A transferase was identified and found to be able to accept five naturally existing H-antigen core structures as good substrates, demonstrating its versatility for synthesis of blood group A antigens. Furthermore, this enzyme was applied in the engineering of bacterial cell surface polysaccharides by remodeling blood group B mimicry into blood group A mimicry. << Less
J Am Chem Soc 130:14420-14421(2008) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.
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Differential recognition of the type I and II H antigen acceptors by the human ABO(H) blood group A and B glycosyltransferases.
Letts J.A., Rose N.L., Fang Y.R., Barry C.H., Borisova S.N., Seto N.O.L., Palcic M.M., Evans S.V.
The human ABO(H) blood group A and B antigens are generated by the homologous glycosyltransferases A (GTA) and B (GTB), which add the monosaccharides GalNAc and Gal, respectively, to the cell-surface H antigens. In the first comprehensive structural study of the recognition by a glycosyltransferas ... >> More
The human ABO(H) blood group A and B antigens are generated by the homologous glycosyltransferases A (GTA) and B (GTB), which add the monosaccharides GalNAc and Gal, respectively, to the cell-surface H antigens. In the first comprehensive structural study of the recognition by a glycosyltransferase of a panel of substrates corresponding to acceptor fragments, 14 high resolution crystal structures of GTA and GTB have been determined in the presence of oligosaccharides corresponding to different segments of the type I (alpha-l-Fucp-(1-->2)-beta-D-Galp-(1-->3)-beta-D-GlcNAcp-OR, where R is a glycoprotein or glycolipid in natural acceptors) and type II (alpha-l-Fucp-(1-->2)-beta-D-Galp-(1-->4)-beta-d-GlcNAcp-OR) H antigen trisaccharides. GTA and GTB differ in only four "critical" amino acid residues (Arg/Gly-176, Gly/Ser-235, Leu/Met-266, and Gly/Ala-268). As these enzymes both utilize the H antigen acceptors, the four critical residues had been thought to be involved strictly in donor recognition; however, we now report that acceptor binding and subsequent transfer are significantly influenced by two of these residues: Gly/Ser-235 and Leu/Met-266. Furthermore, these structures show that acceptor recognition is dominated by the central Gal residue despite the fact that the L-Fuc residue is required for efficient catalysis and give direct insight into the design of model inhibitors for GTA and GTB. << Less
J. Biol. Chem. 281:3625-3632(2006) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
Comments
Citation (not indexed by PubMed): DOI: 10.1021/acscatal.6b02755 J Ye, X Liu, P Peng, W Yi, X Chen, F Wang, H Cao (2016) Diversity-oriented enzymatic modular assembly of ABO histo-blood group antigens. ACS Catalysis, 6, 12, 8140-8144