Alpha-N-acetylgalactosaminidase (NAGA)

Alpha-N-acetylgalactosaminidase (NAGA) is a lysosomal exoglycosidase enzyme that cleaves terminal alpha-N-acetylgalactosamine residues from glycopeptides and glycolipids. It is essential for the stepwise degradation of complex carbohydrates in lysosomes. NAGA functions as a homodimer, possesses a (β/α)8 barrel structure typical of family 27 glycoside hydrolases, and is highly glycosylated and active at acidic pH. Deficiency of NAGA activity leads to accumulation of glycoprotein or glycolipid substrates in cells, resulting in lysosomal storage diseases such as Schindler disease and Kanzaki disease, which are characterized primarily by neurological symptoms and variable severity. Structural and functional analyses illuminate its mechanism, its role in inherited metabolic disorders, and its potential (if inhibited) as a therapeutic target in modulating immune responses and possibly cancer progression[1][2][3].

Other names

Alpha-galactosidase BD22S674GALBAcetylgalactosaminidaseN-acetylgalactosaminidase, alpha-alpha-NAGAL

Enzyme replacement (for deficiency diseases), Inhibition (potential anti-cancer approach by blocking immunosuppressive precursor degradation)[1]