EC Number   |
Natural Substrates |
|---|
   3.5.1.26 | L-asparagine + H2O |
- |
| 3.5.1.26 | L-asparagine + H2O |
low activity |
| 3.5.1.26 | L-asparagine + H2O |
21% activity compared to N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine as substrate |
| 3.5.1.26 | more |
enzyme catalyzes the hydrolysis of the N-glycosylic bond between asparagine and N-acetylglucosamine in the catabolism of N-linked glycoproteins |
| 3.5.1.26 | more |
aspartylglucosaminuria, a lysosomal storage disease caused by mutation L15R, is enriched in the Finnish population |
| 3.5.1.26 | more |
enzyme level in plasma is elevated in congenital disorders of glycosylation type I, CDG I, a defect in biosynthesis or processing of O-linked glycans, overview |
| 3.5.1.26 | more |
AGA hydrolyzes the beta-N glycosidic linkage between the asparagines residue and the N-acetylglucosamine moiety. The enzyme fails to exhibit any glycopeptide N-glycosidase activity toward entire glycoproteins like fetuin, its activity is restricted to the deglycosylation of free glycosylasparagines like human aspartylglucosaminidase |
| 3.5.1.26 | more |
glycosylasparaginase protein is synthesized as a single-chain precursor (inhibitor-free precursor) and requires a cis proteolysis of its own main-chain amide bond, splitting it into two subunits. Once autocleaved, the mature glycosylasparaginase with a free amino end exposed at Thr152 becomes active in glycoprotein degradation by binding to and processing its glycoasparagine substrate |
| 3.5.1.26 | N-[alpha-D-Man-(1-3)-alpha-D-Man-(1-6)-[alpha-D-Man-(1-2)-alpha-D-Man-(1-2)-alpha-D-Man-(1-3)]-beta-D-Man-(1-4)-beta-D-GlcNAc-(1-4)-beta-D-GlcNAc]-L-aspartate + H2O |
fast hydrolysis rate |
| 3.5.1.26 | N4-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-asparagine + H2O |
catabolism of N-linked oligosaccharides |
