136982-79-1Relevant academic research and scientific papers
Synthesis of extended bacterial cell-wall precursor analogues for ligand binding studies with glycopeptide antibiotics
Staroske, Thomas,Goerlitzcr, Jochen,Entrcss, Richard M. H.,Cooper, Matthew A.,Williams, Dudley H.
, p. 1105 - 1107 (2007/10/03)
The synthesis of bacterial cell-wall precursor analogues, which resemble the naturally occurring precursor (lipid II) more closely than those hitherto used in NMR binding studies with glycopeptide antibiotics, is reported.
n-Pentenyl glycosides in the efficient assembly of the blood group substance B tetrasaccharide
Udodong,Rao,Fraser-Reid
, p. 4713 - 4724 (2007/10/02)
The fact that n-pentenyl glycosides (nPGs) are stable to a wide variety of reaction conditions but yet can be chemospecifically activated is advantageous for the efficient, convergent assembly of oligosaccharides. The nPGs are prepared directly from the a
Probing the Acceptor Specificity of β-1,4-Galactosyltransferase for the Development of Enzymatic Synthesis of Novel Oligosaccharides
Wong, Chi-Huey,Ichikawa, Yoshitaka,Krach, Thomas,Narvor, Christine Gautheron-Le,Dumas, David P.,Look, Gary C.
, p. 8137 - 8145 (2007/10/02)
β-1,4-Galactosyltransferase has been investigated with regard to its acceptor specificity and used in the synthesis of galactosides with 5-thioglucose, glucal, deoxynojirimycin, modified N-acetylglucosamine, and glucose derivatives as acceptors. The galactoside products are potentially useful as endoglycosidase or glycosyltransferase inhibitors or as intermediates for the synthesis of complex oligosaccharides. The conformation of each enzyme product has been investigated with NMR; all arc shown to possess similar glycosidic torsional angles based on a significant NOE between H-1 of Gal and H-4 of the acceptor. Comparison of the transferase reactions with the β-1,4-galactosidase-catalyzed galactosyl transfer reactions indicates that the transferase reactions provide exclusively a β-1,4-glycosidic linkage while the galactosidase reactions predominantly form a β-1,6-glycosidic linkage.
