fucosyltransferase

2F-Peracetyl-Fucose (1,3,4-Tri-O-acetyl-2-deoxy-2-fluoro-L-fucopyranos) is a potent fucosyltransferase (FUT) inhibitor that suppresses salivary acidification and fucosylation in an in vitro inflammatory model.

Alpha-1,3 4-Fucosyltransferase (α1,3 4FucT) (Hp3 4FT) is found in Helicobacter pylori and catalyzes the transfer of fucose from donor GDP-beta-l-fucose to the GlcNAc [1].

Fucosyltransferase 2 (EC:2.4.1.69; FUT2) attaches fucose to the terminal galactose of a type I chain via an α1-2 linkage.

Fucosyltransferase 8 (EC:2.4.1.68; FUT8; α1-6FucT) is a glycosyltransferase that catalyzes the transfer of fucose residues from GDP-fucose to the innermost N-acetylglucosamine residue of N-glycans.

Fucosyltransferase 9 (EC:2.4.1.152, FUT9) catalyzes the final step in the biosynthesis of Lewis antigens by adding fucose to precursor polysaccharides. FUT9 synthesizes the LeX oligosaccharide (CD15).

Protein O-Fucosyltransferase 1 (EC:2.4.1.221; POFUT1) is a glycosyltransferase characterized by cysteine-rich motifs serving as receptor sugars and GDP as the donor.

Fucosyltransferase 3 (EC:2.4.1.65, FUT3, FT3B) exhibits potent α 1-3 and α 1-4 fucosyltransferase activity.

Fucosyltransferase 5 (EC:2.4.1.65, Fucosyltransferase 5, Fucosyltransferase V) is responsible for the final step in the synthesis of Lex, sialy-Lex, and Lea antigens.

Focusyltransferase 7 (FUT7) is a Golgi stack membrane protein. It catalyzes the final fucosylation step in the synthesis of Lewis antigens, resulting in the production of the specific glycosylated product sialyl Lewis X (sLeX). FUT7 is involved in catalyzing the α-1,3 glycosidic bond, which is crucial for sialyl Lewis X antigen expression.

Fucosyltransferase 11 (EC:2.4.1.-, FUT11) attaches α-L-fucose to glycoprotein substrates, specifically on asialoglycoprotein glycans and biantennary N-glycan acceptors. This enzyme is significant in the field of oncology.

SGN-2FF is an oral fucosylation inhibitor and inhibits fucosyltransferase activity, and has antitumor activity.

FUT8-IN-1 (Compound 37) is an inhibitor of α-1,6-fucosyltransferase (FUT8), with a dissociation constant (KD) of 49 nM and an IC50 around 50 µM. In the presence of FUT8, FUT8-IN-1 forms a highly active naphthoquinone imine intermediate, thereby inhibiting FUT8's enzymatic activity.

Lacto-N-biose I, also known as Galβ1-3GlcNAc, is a naturally occurring metabolite that serves as a substrate for the α1,2-fucosyltransferase enzyme derived from Helicobacter pylori[1].

FDW028 is a selective and potent fucosyltransferase 8 (FUT8) inhibitor with anti-tumor activity that drives B7-H3 lysosomal degradation via defucosylation and CMA pathways. FUT8 can be used to study metastatic colorectal cancer (mCRC).

Inebilizumab(FUT8-KO) is a modified version of inebilizumab that features a knocked-out fucosyltransferase 8 gene (FUT8). This anti-CD19 monoclonal antibody (mAb) exhibits enhanced antibody-dependent cell-mediated cytotoxicity against B cells, making it suitable for research into multiple sclerosis and neuromyelitis optica.

Petosemtamab (FUT8-KO) is a variant of Petosemtamab with the fucosyltransferase 8 gene (FUT8) knocked out. Petosemtamab is a monoclonal antibody (mAb) targeting EGFR (with a Kd of 0.22 nM) and LGR5 (with a Kd of 0.86 nM). This antibody disrupts EGFR signaling and causes receptor degradation in LGR5+ cancer cells. It is applicable in research on solid tumors such as head and neck squamous cell carcinoma (HNSCC) and metastatic colorectal cancer (CRC).