alpha-(2,6)-Sialyltransferase-catalyzed sialylations of conformationally constrained oligosaccharides.
It is demonstrated that conformationally restricted oligosaccharides can act as acceptors for glycosyltransferases. Correlation of the conformational properties of N-acetyl lactosamine (Galbeta(1-4)GlcNAc, LacNAc) and several preorganized derivatives with the corresponding apparent kinetic parameters of rat liver alpha-(2,6)-sialyltransferase-catalyzed sialylations revealed that this enzyme recognizes LacNAc in a low energy conformation. Furthermore, small variations in the conformational properties of the acceptors resulted in large differences in catalytic efficiency. Collectively, our data suggest that preorganization of acceptors in conformations that are favorable for recognition by a transferase may improve catalytic efficiencies.
Galan
M Carmen
MC
Complex Carbohydrate Research Center, University of Georgia, 220 Riverbend Road, Athens, Georgia 30602, USA.
Venot
Andre P
AP
Glushka
John
J
Imberty
Anne
A
Boons
Geert-Jan
GJ
D000606:Amino Sugars / Q000737:chemistry* / Q000378:metabolism; D002236:Carbohydrate Conformation; D004187:Disaccharides / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D012799:Sialyltransferases / Q000737:chemistry* / Q000378:metabolism; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase
D000606:Amino Sugars; D004187:Disaccharides; C000458:N-acetyllactosamine; D012799:Sialyltransferases; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase