16fucosyltransferases

Fucosyltransferases are a group of enzymes that catalyze the transfer of a fucose monosaccharide from a fucose-donating nucleotide sugar, typically GDP-fucose, to an acceptor molecule. This process is known as fucosylation, a type of glycosylation that is crucial for a variety of biological functions in many organisms. The most commonly studied and biologically significant fucosyltransferases are those involved in the synthesis of fucosylated glycans in humans and other mammals, often referred to as 1,3-fucosyltransferases and 1,6-fucosyltransferases based on the linkage they create.

The 1,6-fucosyltransferases, in particular, are responsible for adding fucose to the innermost N-acetylglucosamine (GlcNAc) residue of N-linked glycans, forming the Lewis a (Le(a)) and Lewis b (Le(b)) antigens, as well as related structures. These enzymes play roles in cell-cell recognition, immune responses, and pathogen binding. For instance, the Lewis antigens are involved in the adhesion of certain bacteria and viruses to host cells. Aberrant expression of these fucosyltransferases has been linked to various disease states, including cancer and inflammatory conditions, making them targets for diagnostic and therapeutic strategies. The human genome encodes several distinct 1,6-fucosyltransferase genes, each with potentially different substrate specificities and tissue distributions, contributing to the diversity of fucosylated glycans found in biological systems.