Fucose mutarotase (FUOM)

Fucose mutarotase is a cytosolic enzyme (EC 5.1.3.29) that catalyzes the reversible interconversion between alpha-L-fucose and beta-L-fucose, two anomeric forms of this essential six-deoxyhexose sugar. This activity is critical for the salvage pathway of GDP-L-fucose biosynthesis, a key donor in cellular fucosylation of glycoproteins and glycolipids. Fucosylated structures are crucial for processes such as cell-cell adhesion, cell recognition, and immune response. In humans, the enzyme is encoded by the FUOM gene; mutations or dysregulation may contribute to congenital disorders of glycosylation and other defects in cell adhesion or metabolism. While not yet established as a direct drug target, fucose mutarotase is under consideration for future therapeutic development due to its central metabolic function and potential disease linkage.

Other names

L-fucose mutarotasefucose 1-epimerasetype-2 mutarotaseFUCMC10orf125FucUA2VDF0EC 5.1.3.29

No clinically established drugs; future small-molecule inhibitors or modulators would alter fucose anomer balance and downstream fucosylation