Glycobiology, 2001, Vol. 11, No. 3 209-216
© 2001 Oxford University Press
Human
3-fucosyltransferases convert chitin oligosaccharides to products containing a GlcNAcß1-4(Fuc
1-3)GlcNAcß1-4R determinant at the nonreducing terminus
Institute of Biotechnology, P.O. Box 56, 00014 University of Helsinki, Finland
Human
3-fucosyltransferases (Fuc-Ts) are known to convert N-acetyllactosamine to Galß1-4(Fuc
1-3)GlcNAc (Lewis x antigen); some of them transfer fucose also to GalNAcß1-4GlcNAc, generating GalNAcß1-4(Fuc
1-3)GlcNAc determinants. Here, we report that recombinant forms of Fuc-TV and Fuc-TVI as well as Fuc-Ts of human milk converted chitin oligosaccharides of 24 GlcNAc units efficiently to products containing a GlcNAcß1-4(Fuc
1-3)GlcNAcß1-4R determinant at the nonreducing terminus. The product structures were identified by mass spectrometry and nuclear magnetic resonance experiments; rotating frame nuclear Overhauser spectroscopy data suggested that the fucose and the distal N-acetylglucosamine are stacked in the same way as the fucose and the distal galactose of the Lewis x determinant. The products closely resembled a nodulation factor of Mesorhizobium loti but were distinct from nodulation signals generated by NodZ-enzyme.
1 Present address: VTT Biotechnology, P.O. Box 1500, 02044 VTT, Finland.
2 To whom correspondence should be addressed
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