PROSITE documentation PDOC51659

Glycosyltransferase family 23 (GT23) domain profile

The fucosylation of glycoconjugates in mammalian organisms is related to a wide 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 α1,2-, α1,3- α1,4-, and α1,6-linkages, and protein O-fucosylation are accomplished by the cation of specific individual fucosyltransferases [1].

FUT8, a eukaryotic α1,6-fucosyltransferase, catalyzes the transfer of a fucosyl residue from guanine nucleotide diphosphate (GDP)-β-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 NodZ, a bacterial α1,6-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 catalyze the α1,6-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 [E1] and share GDP-β-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 [2].

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 (see <PDB:2DE0>) [1,3,4].

The profile we developed covers the entire GT23 domain.