Found 4 structures.
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1. Compound ID: 40
Structure type: oligomer
Contained glycoepitopes: IEDB_136044,IEDB_136045,IEDB_137472,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_142489,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_150948,IEDB_152214,IEDB_153553,IEDB_153555,IEDB_174333,IEDB_190606,IEDB_461719,IEDB_983931,SB_154,SB_165,SB_166,SB_187,SB_192,SB_195,SB_6,SB_7,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 16
Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" -
Glycobiology 9(10) (1999) 1061-1071
We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.
oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase
NCBI PubMed ID: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
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2. Compound ID: 6048
Structure type: oligomer
Compound class: LPS
Contained glycoepitopes: IEDB_136044,IEDB_136045,IEDB_137472,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_142489,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_150948,IEDB_152214,IEDB_153553,IEDB_153555,IEDB_174333,IEDB_190606,IEDB_461719,IEDB_983931,SB_154,SB_165,SB_166,SB_187,SB_192,SB_195,SB_6,SB_7,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 2694
Bryn K, Jantzen E "Quantification of 2-keto-3-deoxyoctonate in (lipo)polysaccharides by methanolytic release, trifluoroacetylation and capillary gas chromatography" -
Journal of Chromatography 370 (1986) 103-112
Several conditions of acidic anhydrous methanolysis were examined to optimize the release and minimize the degradation of unphosphorylated 2-keto-3-deoxy-D-manno-octonic acid (KDO) from bacterial lipopolysaccharides and polysaccharides. The reaction was monitored by capillary gas chromatography after derivatization by trifluoroacetic anhydride. The best results were obtained by use of 2 M hydrochloric acid at 60 degrees C for 2 h. Under these conditions a single KDO component appeared, and KDO was quantitatively released from all model compounds except when glycosidically linked to hexosamines. For quantitative cleavage of this linkage a reaction time of 6 h was required at 60 degrees C, giving rise to 5-10% of secondary KDO products. The KDO detection limit was about 250 pmol (50 ng) and the molar response was the same as for glucose. The KDO derivative gave a mass spectrometric fragmentation pattern consistent with a pyranosidic methylketoside methyl ester structure. Differentiation of KDO linkage types could be obtained by determination of the rates of KDO release by mild methanolysis.
NCBI PubMed ID: 3805213Journal NLM ID: 0427043Publisher: Amsterdam: Elsevier
Methods: GC-MS, MS
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3. Compound ID: 6261
Structure type: oligomer
Contained glycoepitopes: IEDB_130648,IEDB_136044,IEDB_136045,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_140124,IEDB_141584,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_142489,IEDB_144562,IEDB_144998,IEDB_145670,IEDB_146664,IEDB_150948,IEDB_152213,IEDB_152214,IEDB_152218,IEDB_153205,IEDB_153206,IEDB_153553,IEDB_153554,IEDB_153555,IEDB_156996,IEDB_174039,IEDB_174333,IEDB_190606,IEDB_2151202,IEDB_461719,IEDB_885822,IEDB_983931,SB_149,SB_154,SB_165,SB_166,SB_187,SB_192,SB_195,SB_21,SB_6,SB_7,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 2826
Gaffar A, Gibbons RJ, Tylewksa S "Oral compositions containing oligosaccharide for inhibition of Streptococcus pyogenes adhesion on oral cells" -
USA Patent Applications (1991) 1-5
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4. Compound ID: 30915
Structure type: oligomer
Compound class: oligosaccharide
Contained glycoepitopes: IEDB_136044,IEDB_136045,IEDB_137472,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_142489,IEDB_144562,IEDB_146664,IEDB_150948,IEDB_152214,IEDB_153553,IEDB_153555,IEDB_174333,IEDB_190606,IEDB_461719,IEDB_983931,SB_154,SB_165,SB_166,SB_187,SB_192,SB_195,SB_6,SB_7,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 11842
Dunand C, Gautier C, Chambat G, Lienart Y "Characterization of the binding of α-L-Fuc(1→2)-β-D-Gal(1→), a xyloglucan signal, in blackberry protoplasts" -
Plant Science 151(2) (2000) 183-192
Previous work showed that the fucose1→galactose moiety of the xyloglucan nonasaccharide XXFG is responsable for its biological activity. We used this side chain of XXFG (α-L-Fuc(1→2)-β-D-Gal(1→)) in ligand-binding experiments to demonstrate its role as a signal molecule in plant cells. Proteins solubilized from plasma membrane enriched fractions isolated from Rubus fruticosus protoplasts were tested for their ability to bind the side chain of XXFG, using a digoxigenin- or biotin-conjugated neoglycoprotein specific for 2'-fucosyl-lactose in blots and k-ELISA tests. A putative receptor for the signaling sugar was identified, and the ligand specificity is reported. The role of structural elements important for biological activities was investigated using compounds structurally related to xyloglucan, and a variety of phytohormones such as 2,4-D.
protoplasts, xyloglucan, [α-L-Fuc(1→2)-β-D-Gal(1→)] signal, Rubus fruticosis
NCBI PubMed ID: 10808074Publication DOI: 10.1016/s0168-9452(99)00217-4Publisher: Elsevier
Correspondence: lienart@cermav.cnrs.fr
Institutions: CERMAV-CNRS, Laboratoire associeé á l'Université Joseph Fourier, Grenoble, France
Methods: deacetylation, SDS-PAGE, ELISA, biological assays, extraction, binding assays, dialysis, enzymatic assay, derivatization, Bradford method, centrifugation
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