| Description | The fucosylation of glycoconjugates in mammalian organisms is related to a wide variety of biological processes, 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 a fucosyl residue from guanine nucleotide diphosphate (GDP)-beta-L-fucose to the reducing terminal N-acetylglucosamine (GlcNAc) of asparagine-linked oligosaccharides (N-glycan). The catalytic domain of FUT8 is structurally similar to that of BodZ, a bacterial alpha1,6-fucosyltransferase. NodZ plays a role in the synthesis of the Nod factor, which is involved in the nodulation of legume roots for nitrogen fixing, and is known to catalyse the alpha1,6- fucosylation of lipo-chitooligosaccharides and variations thereof, including chitooligosaccharides. Both the eukaryotic and bacterial fucoslytransferase are 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 α/β structure and a C-terminal Rossmann fold which is frequently found in nucleotide binding proteins including glycosyltransferases [ , , ]. The entry represents the GT23 domain. | Name | Glycosyltransferase family 23 (GT23) domain |
| Short Name | GT23_dom | Type | Domain |
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