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| Subject | Predicate | Object |
|---|---|---|
| http://purl.uniprot.org/citations/16157350 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16157350 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16157350 | http://www.w3.org/2000/01/rdf-schema#comment | "beta-1,4-Galactosyltransferase-I (beta4Gal-T1) transfers galactose from UDP-galactose to N-acetylglucosamine (GlcNAc) residues of the branched N-linked oligosaccharide chains of glycoproteins. In an N-linked biantennary oligosaccharide chain, one antenna is attached to the 3-hydroxyl-(1,3-arm), and the other to the 6-hydroxyl-(1,6-arm) group of mannose, which is beta-1,4-linked to an N-linked chitobiose, attached to the aspargine residue of a protein. For a better understanding of the branch specificity of beta4Gal-T1 towards the GlcNAc residues of N-glycans, we have carried out kinetic and crystallographic studies with the wild-type human beta4Gal-T1 (h-beta4Gal-T1) and the mutant Met340His-beta4Gal-T1 (h-M340H-beta4Gal-T1) in complex with a GlcNAc-containing pentasaccharide and several GlcNAc-containing trisaccharides present in N-glycans. The oligosaccharides used were: pentasaccharide GlcNAcbeta1,2-Manalpha1,6 (GlcNAcbeta1,2-Manalpha1,3)Man; the 1,6-arm trisaccharide, GlcNAcbeta1,2-Manalpha1,6-Manbeta-OR (1,2-1,6-arm); the 1,3-arm trisaccharides, GlcNAcbeta1,2-Manalpha1,3-Manbeta-OR (1,2-1,3-arm) and GlcNAcbeta1,4-Manalpha1,3-Manbeta-OR (1,4-1,3-arm); and the trisaccharide GlcNAcbeta1,4-GlcNAcbeta1,4-GlcNAc (chitotriose). With the wild-type h-beta4Gal-T1, the K(m) of 1,2-1,6-arm is approximately tenfold lower than for 1,2-1,3-arm and 1,4-1,3-arm, and 22-fold lower than for chitotriose. Crystal structures of h-M340H-beta4Gal-T1 in complex with the pentasaccharide and various trisaccharides at 1.9-2.0A resolution showed that beta4Gal-T1 is in a closed conformation with the oligosaccharide bound to the enzyme, and the 1,2-1,6-arm trisaccharide makes the maximum number of interactions with the enzyme, which is in concurrence with the lowest K(m) for the trisaccharide. Present studies suggest that beta4Gal-T1 interacts preferentially with the 1,2-1,6-arm trisaccharide rather than with the 1,2-1,3-arm or 1,4-1,3-arm of a bi- or tri-antennary oligosaccharide chain of N-glycan."xsd:string |
| http://purl.uniprot.org/citations/16157350 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jmb.2005.07.050"xsd:string |
| http://purl.uniprot.org/citations/16157350 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jmb.2005.07.050"xsd:string |
| http://purl.uniprot.org/citations/16157350 | http://purl.uniprot.org/core/author | "Ramakrishnan B."xsd:string |
| http://purl.uniprot.org/citations/16157350 | http://purl.uniprot.org/core/author | "Ramakrishnan B."xsd:string |
| http://purl.uniprot.org/citations/16157350 | http://purl.uniprot.org/core/author | "Seeberger P.H."xsd:string |
| http://purl.uniprot.org/citations/16157350 | http://purl.uniprot.org/core/author | "Seeberger P.H."xsd:string |
| http://purl.uniprot.org/citations/16157350 | http://purl.uniprot.org/core/author | "Ratner D.M."xsd:string |
| http://purl.uniprot.org/citations/16157350 | http://purl.uniprot.org/core/author | "Ratner D.M."xsd:string |
| http://purl.uniprot.org/citations/16157350 | http://purl.uniprot.org/core/author | "Boeggeman E."xsd:string |
| http://purl.uniprot.org/citations/16157350 | http://purl.uniprot.org/core/author | "Boeggeman E."xsd:string |
| http://purl.uniprot.org/citations/16157350 | http://purl.uniprot.org/core/author | "Qasba P.K."xsd:string |
| http://purl.uniprot.org/citations/16157350 | http://purl.uniprot.org/core/author | "Qasba P.K."xsd:string |
| http://purl.uniprot.org/citations/16157350 | http://purl.uniprot.org/core/author | "Ramasamy V."xsd:string |
| http://purl.uniprot.org/citations/16157350 | http://purl.uniprot.org/core/author | "Ramasamy V."xsd:string |
| http://purl.uniprot.org/citations/16157350 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16157350 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16157350 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/16157350 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/16157350 | http://purl.uniprot.org/core/pages | "53-67"xsd:string |
| http://purl.uniprot.org/citations/16157350 | http://purl.uniprot.org/core/pages | "53-67"xsd:string |
| http://purl.uniprot.org/citations/16157350 | http://purl.uniprot.org/core/title | "Oligosaccharide preferences of beta1,4-galactosyltransferase-I: crystal structures of Met340His mutant of human beta1,4-galactosyltransferase-I with a pentasaccharide and trisaccharides of the N-glycan moiety."xsd:string |
| http://purl.uniprot.org/citations/16157350 | http://purl.uniprot.org/core/title | "Oligosaccharide preferences of beta1,4-galactosyltransferase-I: crystal structures of Met340His mutant of human beta1,4-galactosyltransferase-I with a pentasaccharide and trisaccharides of the N-glycan moiety."xsd:string |