Human alpha3-fucosyltransferases (Fuc-Ts) are known to convert N-acetyllactosamine to Gal beta1-4(Fuc alpha1-3)GlcNAc (Lewis x antigen); some of them transfer fucose also to GalNAc beta1-4GlcNAc, generating GalNAc beta1-4(Fuc alpha1-3)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 2-4 GlcNAc units efficiently to products containing a GlcNAc beta1-4(Fuc alpha1-3)GlcNAc beta1-4R 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.
|Number of pages||8|
|Publication status||Published - 2001|
|MoE publication type||A1 Journal article-refereed|
Natunen, J., Aitio, O., Helin, J., Maaheimo, H., Niemelä, R., Heikkinen, S., & Renkonen, O. (2001). Human alfa3-fucosyltransferases convert chitin oligosaccharides to products containing a GlcNacbeta1-4(Fucalfa1-3)GlcNAc beta1-4R determinant at the nonreducing terminus. Glycobiology, 11(3), 209-216.