Porcine liver (2-->3)-alpha-sialyltransferase: substrate specificity studies and application of the immobilized enzyme to the synthesis of various sialylated oligosaccharide sequences.
In search of substrate analogues for the porcine liver beta-D-Gal p-(1-->3)-D-Gal p-NAc: CMP-Neu5Ac-(2-->3')-alpha-sialyltransferase, three disaccharides beta-D-Gal p-(1-->3)-beta-D-Gal p-O-CH3 (5), beta-D-Gal p-(1-->3)-beta-D-(2-OAc)-Gal p-O-CH3 (7) and beta-D-Gal p-(1-->3)-beta-D-(2-OAc)-Gal p-O-Bn (11) were synthesized and tested with the enzyme. Disaccharide 7 turned out to be a very good substrate allowing a rapid access to the trisaccharide alpha-Neu5Ac-(2-->3)-beta-D-Gal p-(1-->3)-beta-D-(2-OAc)-Gal p-O-CH3 (13) on a preparative scale using the crude enzyme immobilized on cationic exchanger. Trisaccharide 13 was further exploited, first as a sialyl donor in Trypanosoma cruzi trans-sialidase catalyzed reaction and second through acetolysis reaction as a source for the synthon alpha-Neu5Ac-(2-->3)-D-Gal (16).
Lubineau
A
A
Institut de Chimie Moléculaire d'Orsay, U.R.A. C.N.R.S. 462, Université de Paris-Sud, France.
Basset-Carpentier
K
K
Augé
C
C
D000818:Animals; D002240:Carbohydrate Sequence; D004800:Enzymes, Immobilized / Q000737:chemistry*; D008099:Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000138:chemical synthesis / Q000737:chemistry*; D012799:Sialyltransferases / Q000737:chemistry* / Q000378:metabolism; D013379:Substrate Specificity; D013552:Swine
D004800:Enzymes, Immobilized; D009844:Oligosaccharides; D012799:Sialyltransferases