Enzymes
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- Name help_outline a ganglioside GM3 (d18:1(4E)) Identifier CHEBI:60065 Charge -1 Formula C42H72N2O21R 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@@]3(C[C@H](O)[C@@H](NC(C)=O)[C@@H](O3)[C@H](O)[C@H](O)CO)C([O-])=O)[C@H]2O)[C@H](O)[C@H]1O)NC([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 8 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 38 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a β-D-GalNAc-(1→4)-α-Neu5Ac-(2→3)-β-D-Gal-(1→4)-β-D-Glc-(1↔1)-Cer Identifier CHEBI:57646 Charge -1 Formula C50H85N3O26R SMILEShelp_outline [H][C@]1(O[C@@](C[C@H](O[C@@H]2O[C@H](CO)[C@H](O)[C@H](O)[C@H]2NC(C)=O)[C@H]1NC(C)=O)(O[C@H]1[C@@H](O)[C@@H](CO)O[C@@H](O[C@H]2[C@H](O)[C@@H](O)[C@H](OC[C@H](NC([*])=O)[C@H](O)\C=C\CCCCCCCCCCCCC)O[C@@H]2CO)[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 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 9,176 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 542 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:13569 | RHEA:13570 | RHEA:13571 | RHEA:13572 | |
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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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Identification and characterization of UDP-GalNAc: NeuAc alpha 2-3Gal beta 1-4Glc(NAc) beta 1-4(GalNAc to Gal)N-acetylgalactosaminyltransferase in human blood plasma.
Takeya A., Hosomi O., Kogure T.
Normal human plasma was found to contain beta 1-4N-acetylgalactosaminyltransferase catalyzing the transfer of N-acetylgalactosamine from UDP-GalNAc to 3'-sialyl-lactose, NeuAc alpha 2-3Gal beta 1-4Glc. The transferred N-acetylgalactosaminyl residue was cleaved from the desialylated reaction produc ... >> More
Normal human plasma was found to contain beta 1-4N-acetylgalactosaminyltransferase catalyzing the transfer of N-acetylgalactosamine from UDP-GalNAc to 3'-sialyl-lactose, NeuAc alpha 2-3Gal beta 1-4Glc. The transferred N-acetylgalactosaminyl residue was cleaved from the desialylated reaction product by the beta-N-acetylhexosaminidase from jack beans. Methylation and hydrolysis of the desialylated reaction product yielded only 2,3,6-tri-O-methylgalactose and 2,3,6-tri-O-methylglucose as neutral sugars, indicating that the N-acetylgalactosaminyl residue was introduced at position C-4 of the galactosyl residue of 3'-sialyllactose. The enzyme required Mn2+ ions for its activity and showed a pH optimum between 6.5 and 8.5. By using a wide variety of oligosaccharides and glycoconjugates, the acceptor specificity of the beta 1-4N-acetylgalactosaminyltransferase was investigated. No detectable amount of N-acetylgalactosamine was transferred to either 6'-sialyllactose or lactose. The enzyme did not act on ganglioside GM3, NeuAc alpha 2-3Gal beta 1-4Glc-ceramide, suggesting that the hydrophobic ceramide portion of GM3 interferes with the enzyme reaction. On the other hand, glycoproteins carrying terminal NeuAc alpha 2-3Gal beta 1-4GlcNAc structures on their N-linked oligosaccharide chains, e.g. Tamm-Horsfall glycoprotein, were efficient acceptors. << Less
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Identification of a alpha-NeuAc-(2----3)-beta-D-galactopyranosyl N-acetyl-beta-D-galactosaminyltransferase in human kidney.
Piller F., Blanchard D., Huet M., Cartron J.P.
Microsomal preparations from human kidney were found to contain enzymic activity capable to transfer N-acetylgalactosamine from UDP-N-acetylgalactosamine to native bovine fetuin. The acceptor structures on the fetuin molecules were identified as N-as well as O-linked glycans with a markedly higher ... >> More
Microsomal preparations from human kidney were found to contain enzymic activity capable to transfer N-acetylgalactosamine from UDP-N-acetylgalactosamine to native bovine fetuin. The acceptor structures on the fetuin molecules were identified as N-as well as O-linked glycans with a markedly higher incorporation into the N-linked carbohydrate chains. Analysis of the alkali-labile transferase products by thin-layer chromatography indicated that the enzyme is able to synthesize structures having mobilities identical with those found on glycophorin from Cad erythrocytes. Mild acid treatment and enzymic hydrolysis with N-acetylhexosaminidase from jack beans of the N-linked transferase products suggested that beta-D-GalpNAc-(1----4)-[alpha-NeuAc-(2----3)]-beta-D-Galp-(1----s tructures were formed by the enzymic reaction on both N- and O-linked acceptors. The enzyme might, therefore, be involved in the biosynthesis of Sda (and Cad) antigenic structures. By use of various oligosaccharides, glycopeptides, and glycolipids having well characterized carbohydrate sequences, the acceptor-substrate specificity of the N-acetylgalactosaminyltransferase was determined. The enzyme generally recognized alpha-NeuAc-(2----3)-beta-D-Gal groups as acceptors, but in a certain conformation. Thus, tri- and tetra-saccharide alditols, native human glycophorin A, and GM3 were not acceptor substrates although they carry the potential disaccharide acceptor unit. When these structures were presented as sialyl-(2----3)-lactose or as a tryptic peptide from glycophorin A, they were shown to be rather good acceptor substrates for the N-acetyl-beta-D-galactosaminyltransferase from human kidney. << Less
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Biosynthesis of a globoside-type glycosphingolipid by a -N-acetylgalactosaminyltransferase from embryonic chicken brain.
Chien J.L., Williams T., Basu S.
J Biol Chem 248:1778-1785(1973) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.