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Fucosyltransferase 9 (FUT9) is an α1,3-fucosyltransferase enzyme that catalyzes the transfer of fucose from GDP-fucose to N-acetyl-lactosamine acceptors, generating fucosylated glycan structures such as Lewis X (LeX/CD15) and stage-specific embryonic antigen-1 (SSEA-1)[2][3]. It preferentially acts on type 2 lactosamine and related structures on glycolipids and glycoproteins, including lysosome-associated membrane protein 1 (LAMP-1) in neural tissues[1][4]. FUT9 plays a critical role in neural development, particularly in the generation of Lewis X in the brain; Fut9 knockout mice exhibit absence of brain LeX and altered neuronal function[2][3]. In cancer, FUT9 expression can drive changes in the cell surface glycome, affecting cell adhesion and metastatic potential[2][3]. Structurally, FUT9 has a GT-B glycosyltransferase fold with distinct donor and acceptor binding domains and forms a dimer[1]. There are no drugs currently approved as direct FUT9 inhibitors or modulators; its primary biomedical significance is as a mediator of protein and lipid glycosylation relevant to neurobiology and oncology[3][2].
Enzymatic transfer of fucose from GDP-fucose to N-acetylglucosamine-containing glycan acceptors (α1,3-fucosylation)
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