Aglycone structure influences α-fucosyltransferase III activity using N-acetyllactosamine glycoside acceptors
- 1 January 1999
- journal article
- Published by Springer Nature in Glycoconjugate Journal
- Vol. 16 (11) , 725-730
- https://doi.org/10.1023/a:1007163510870
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.Keywords
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