Alpha-L-fucosidase 2 (FUCA2)

Alpha-L-fucosidase 2 (FUCA2) is a secreted enzyme responsible for the removal of terminal fucose residues from glycoproteins and other glycoconjugates, playing a critical role in modulating extracellular glycan structures[1][3]. It is a member of the glycosyl hydrolase 29 family and catalyzes the hydrolysis of alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of carbohydrate moieties. The enzyme is essential for microbial adhesion, such as facilitating Helicobacter pylori binding in gastric tissues. FUCA2 is also upregulated in several cancers (correlating with poor prognosis and immunosuppression), linked to cardiovascular dysfunctions, and participates in immune cell signaling[1][3]. Its expression can be modulated by cytokines like interferon-gamma, suggesting a broader role in immune response and disease pathogenesis[1][3].

Other names

Plasma alpha-L-fucosidasePSEC0151UNQ227/PRO260Alpha-L-fucosidase 2MGC1314dJ20N2.5Alpha-L-fucoside fucohydrolase 2α-L-fucosidase 2plasma fucosidasea-L-fucosidase 2

Enzymatic hydrolysis of terminal alpha-1,6-linked fucose residues from glycoproteins and glycoconjugates[1][3]