Enzymes
| UniProtKB help_outline | 595 proteins |
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- Name help_outline an N-acetyl-β-D-glucosaminyl derivative Identifier CHEBI:61631 Charge 0 Formula C8H14NO6R SMILEShelp_outline O1[C@@H]([C@H]([C@@H]([C@H]([C@@H]1O*)NC(=O)C)O)O)CO 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline UDP-α-D-galactose Identifier CHEBI:66914 Charge -2 Formula C15H22N2O17P2 InChIKeyhelp_outline HSCJRCZFDFQWRP-ABVWGUQPSA-L SMILEShelp_outline OC[C@H]1O[C@H](OP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2ccc(=O)[nH]c2=O)[C@H](O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 105 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl derivative Identifier CHEBI:133507 Charge 0 Formula C14H24NO11R SMILEShelp_outline [C@@H]1([C@@H]([C@H]([C@H]([C@H](O1)CO)O)O)O)O[C@H]2[C@@H]([C@H]([C@@H](O[C@@H]2CO)O*)NC(=O)C)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 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 9,431 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 576 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:22932 | RHEA:22933 | RHEA:22934 | RHEA:22935 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
Specific form(s) of this reaction
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RHEA:56260
N4-{β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-asparaginyl-[protein] + 4 UDP-α-D-galactose = 4 H+ + N4-{β-D-Gal-(1→4)-β-D-GlcNAc-(1→2)-[β-D-Gal-(1→4)-β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-Gal-(1→4)-β-D-GlcNAc-(1→2)-[β-D-Gal-(1→4)-β-D-GlcNAc-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-asparaginyl-[protein] + 4 UDP
Publications
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Biosynthesis of blood-group I and i substances. Specificity of bovine colostrum beta-N-acetyl-D-glucosaminide beta 1 leads to 4 galactosyltransferase.
Blanken W.M., Hooghwinkel G.J., Van Den Eijnden D.H.
Highly purified bovine colostrum beta-N-acetylglucosaminide beta 1 leads to 4 galactosyltransferase was used to investigate the galactosylation of the synthetic, branched trisaccharide GlcNAcbeta 1 leads to 3(GlcNAcbeta 1 leads to 6)Gal, which is the branching point in blood-group I antigenic stru ... >> More
Highly purified bovine colostrum beta-N-acetylglucosaminide beta 1 leads to 4 galactosyltransferase was used to investigate the galactosylation of the synthetic, branched trisaccharide GlcNAcbeta 1 leads to 3(GlcNAcbeta 1 leads to 6)Gal, which is the branching point in blood-group I antigenic structures. Two galactose residues could readily be incorporated from UDP-galactose into the trisaccharide, yielding a pentasaccharide with the following structure: Galbeta 1 leads to 4GlcNAcbeta 1 leads to 3(Galbeta 1 leads to 4GlcNAcbeta 1 leads to 6)Gal. From a partially completed incubation an intermediate tetrasaccharide was isolated, the structure of which was investigated by use of an acetolysis method, involving high-pressure liquid chromatography and double labelling techniques. It appeared that this intermediate consisted for more than 95% of one of two possible structures: GlcNAcbeta 1 leads to 3(Galbeta 1 leads to 4GlcNAcbeta 1 leads to 6)Gal. This reveals that the enzymatic galactosylation of the trisaccharide proceeds in a highly preferred order, in which the 1 leads to 6-linked N-acetylglucosamine residue is galactosylated first and thus that the galactosyltransferase displays a high degree of 'branch specificity'. Kinetic data suggest that galactosylation of the 1 leads to 6-linked N-acetylglucosamine in the trisaccharide enhances the acceptor properties of the 1 leads to 3-linked N-acetylglucosamine residue. << Less
Eur J Biochem 127:547-552(1982) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Biosynthesis of terminal Gal alpha 1----3Gal beta 1----4GlcNAc-R oligosaccharide sequences on glycoconjugates. Purification and acceptor specificity of a UDP-Gal:N-acetyllactosaminide alpha 1----3-galactosyltransferase from calf thymus.
Blanken W.M., Van den Eijnden D.H.
A UDP-Gal:Gal beta 1----4GlcNAc-R alpha 1----3- and a UDP-Gal:GlcNAc-R beta 1----4-galactosyltransferase have been purified 44,000- and 101,000-fold, respectively, from a Triton X-100 extract of calf thymus by affinity chromatography on UDP-hexanolamine-Sepharose and alpha-lactalbumin-Sepharose in ... >> More
A UDP-Gal:Gal beta 1----4GlcNAc-R alpha 1----3- and a UDP-Gal:GlcNAc-R beta 1----4-galactosyltransferase have been purified 44,000- and 101,000-fold, respectively, from a Triton X-100 extract of calf thymus by affinity chromatography on UDP-hexanolamine-Sepharose and alpha-lactalbumin-Sepharose in a yield of 25-40%. Sodium dodecyl sulfate gel electrophoresis under reducing conditions revealed a major polypeptide species with a molecular weight of 40,000 and a minor form at Mr 42,000 for the alpha 1----3-galactosyltransferase and a major polypeptide with Mr 51,000 for the beta 1----4-galactosyltransferase. Analytical gel filtration on Sephadex G-100 yielded a monomeric form for each of the galactosyltransferases with Mr 43,000 and 59,000 respectively, in addition to peaks of activity at higher molecular weights. Isoelectric focussing of the alpha 1----3-galactosyltransferase revealed a significant charge heterogeneity with forms varying in pI values between 5.0 and 6.5. Acceptor specificity studies indicated that the purified alpha 1----3-galactosyltransferase was free from contaminating galactosyltransferase activities such as those involved in the synthesis of Gal beta 1----4GlcNAc-R and Gal beta 1----3GalNAc-R sequences, the blood group B determinant, the Pk antigen, trihexosylceramide, and ganglioside GM1. The alpha 1----3-galactosyltransferase appeared to be highly active with glycoproteins, oligosaccharides, and glycolipids having a terminal Gal beta 1----4GlcNAc beta 1----unit such as asialo-alpha 1-acid glycoprotein (Km = 1.25 mM), Gal beta 1----4GlcNAc beta 1----2Man alpha 1----3Man beta 1----4GlcNAc (Km = 0.57 mM), and paragloboside. The action of the alpha 1----3-galactosyltransferase was found to be mutually exclusive with that of the NeuAc:Gal beta 1----4GlcNAc-R alpha 2----6-sialyltransferase from bovine colostrum. In addition alpha 1----3-fucosylation of the N-acetylglucosamine residue in the preferred disaccharide acceptor structure completely blocked galactosylation of the alpha 1----3-galactosyltransferase. << Less
J Biol Chem 260:12927-12934(1985) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Glycosyltransferases and their use in assessing oligosaccharide structure and structure-function relationships.
Beyer T.A., Sadler J.E., Rearick J.I., Paulson J.C., Hill R.L.
Adv Enzymol Relat Areas Mol Biol 52:23-175(1981) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.