Aspartylglucosaminidase (AGA)

Aspartylglucosaminidase is a lysosomal amidohydrolase enzyme responsible for cleaving the bond between asparagine and N-acetylglucosamine in N-linked glycoproteins during the final steps of lysosomal degradation. It is synthesized as a single precursor chain, which undergoes post-translational cleavage to produce α and β subunits that assemble into a functional heterotetramer. Deficiency of this enzyme activity, typically due to mutations in the AGA gene, leads to aspartylglucosaminuria—a lysosomal storage disorder characterized by progressive intellectual disability and motor impairments resulting from disrupted glycoprotein catabolism and subsequent accumulation in neural and other tissues[1][2][3][4][5].

Other names

GlycosylasparaginaseN(4)-(beta-N-acetylglucosaminyl)-L-asparaginaseN4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidaseAspartylglucosylamine deaspartylaseASRGGAAGU