ISSN:
1573-4986
Keywords:
substrate specificity
;
fucosyltransferase
;
glycosides
;
N-acetyllactosamine
;
N-acetylglucosaminides
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract We showed previously that Chinese hamster ovary cells took up and utilized a variety of N-acetylglucosaminides as primers of oligosaccharide biosynthesis (Ding et al., 1999, J. Carbohydr. Chem., 18:471–475). In this study, a library of N-acetylglucosaminides was enzymatically galactosylated in vitro to yield type 2 chain N-acetyllactosaminides bearing a variety of aglycones. Those disaccharides are potential acceptors for fucosyltransferases. As an extension of the previous study, we tested the type 2 chain disaccharyl glycosides (Galβ1,4-GlcNAcβ-R) for their aglycone-dependent acceptor specificity for α-L-fucosyltransferase III (Fuc-TIII). The enzyme activity significantly depended on the aglycone structures, suggesting that, in addition to the polar groups on the sugar moiety, the hydrophobic aglycone can substantially contribute to recognition in this reaction.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1007163510870
Permalink
