NAGA (alpha-N-acetylgalactosaminidase) is a lysosomal exoglycosidase that removes terminal alpha-N-acetylgalactosamine residues from glycolipids and glycopeptides, playing a critical role in glycolipid catabolism 1. The enzyme functions as a homodimer and operates through a carbohydrate catabolic pathway involving glycoside hydrolysis [GO Annotations]. NAGA shares structural similarity with alpha-galactosidase A (α-GAL A), including dual active sites capable of binding diverse substrates such as alpha-D-galactose and N-acetyl-D-galactosamine 2. Pathogenic mutations in NAGA cause Schindler disease and Kanzaki disease, rare lysosomal storage disorders characterized by progressive glycolipid accumulation in tissues. Clinically, NAGA has emerged as a promising therapeutic target for Fabry disease; modified NAGA variants demonstrate efficacy as enzyme replacement therapy candidates, suppressing globotriaosylceramide and globotriaosylsphingosine accumulation while avoiding antidrug antibody formation that limits conventional alpha-galactosidase A therapy 1. These properties position NAGA as both a biomarker for storage diseases and a potential therapeutic protein for glycosphingolipidoses.