| Primary Identifier | IPR027350 | Type | Domain |
| Short Name | GT23_dom |
| description | The fucosylation of glycoconjugates in mammalian organisms is related to awide variety of biological preocesses, including cell adhesion, blood antigens, and some severe diseases including cancer metastasis, congenital disorders of glycosylation, and various microbial and virus infections. Fucosylation via alpha1,2-, alpha1,3- alpha1,4, and alpha1,6-linkages, and protein O-fucosylation are accomplished by the cation of specific individual fucosyltransferases [].FUT8, a eukaryotic alpha1,6-fucosyltransferase, catalyses the transfer of afucosyl residue from guanine nucleotide diphosphate (GDP)-beta-L-fucose to thereducing terminal N-acetylglucosamine (GlcNAc) of asparagine-linkedoligosaccharides (N-glycan). The catalytic domain of FUT8 is structurallysimilar to that of BodZ, a bacterial alpha1,6-fucosyltransferase. NodZ plays arole in the synthesis of the Nod factor, which is involved in the nodulationof legume roots for nitrogen fixing, and is known to catalyse the alpha1,6-fucosylation of lipo-chitooligosaccharides and variations thereof, includingchitooligosaccharides. Both the eukaryotic and bacterial fucoslytransferaseare classified into the GT23 family of Carbohydrate-Active enZYmes and share GDP-beta-L-fucose as the donor substrate. Although the acceptor substrates are different, a "common"chitobiose unit is contained in the reducing terminals of both substrates [].The GT23 domain is comprised of two structures, a N-terminal open sheet alpha/beta structure and a C-terminal Rossmann fold which is frequently found innucleotide binding proteins including glycosyltransferases[, , ]. The entry represents the GT23 domain. |
