EC Number   |
General Information |
Reference |
|---|
   3.5.1.26 | evolution |
belongs to the group of so-called N-terminal nucleophile (NTN) hydrolases. The members of the NTN hydrolase family, which in addition to AGA also include, e.g., the proteasome beta-subunit and penicillin acylase, show very little similarity at the amino acid sequence level, but they exhibit a highly similar folded structure |
753910 |
| 3.5.1.26 | evolution |
molecular phylogenetic analysis of aspartylglucosaminidases |
753910 |
| 3.5.1.26 | evolution |
the venom AGAs have a similar domain organization as mammalian AGAs. They share key residues for autocatalysis and activity, and the mature alpha- and beta-subunits also form an (alphabeta)2 structure in solution. Only one of the AGAs subunits, the beta for LhAGA, is glycosylated instead of the two subunits for lysosomal human AGA (hAGA) |
755152 |
| 3.5.1.26 | evolution |
the venom AGAs have a similar domain organization as mammalian AGAs. They share with them key residues for autocatalysis and activity, and the mature alpha- and beta-subunits also form an (alphabeta)2 structure in solution. Only one of the AGAs subunits (alpha for AtAGA) is glycosylated instead of the two subunits for lysosomal human AGA (hAGA) |
755152 |
| 3.5.1.26 | malfunction |
aspartylglucosaminuria (AGU) is an inherited disease caused by mutations in a lysosomal amidase called aspartylglucosaminidase (AGA) or glycosylasparaginase. This disorder results in an accumulation of glycoasparagines in the lysosomes of virtually all cell types, with severe clinical symptoms affecting the central nervous system, skeletal abnormalities, and connective tissue lesions. Many AGU mutations remain as dimers but cannot undergo autoproteolysis and thus lack amidase activity for digesting glycoasparagines |
755339 |
| 3.5.1.26 | malfunction |
aspartylglycosaminuria is a lysosomal storage disease caused by deficient activity of glycosylasparaginase |
712651 |
| 3.5.1.26 | malfunction |
defects in the AGA gene result in a lysosomal storage disorder, aspartylglucosaminuria (AGU), that manifests mainly as progressive mental retardation. A number of AGU missense mutations have been identified that result in reduced AGA activity. Human variants contain either Ser or Thr in position 149, and Thr149 AGA, which is the rare variant, can be considered as a neutral or benign variant. AGU mutations result in reduced AGA activity in patient cells. Mutations in the AGA gene result in aspartylglucosaminuria (AGU, OMIM 208400), a lysosomal storage disorder that is characterized by progressive loss of intellectual capabilities and some skeletal abnormalities. AGU patients are born seemingly normal, but the progressive course of the disease manifests in, e.g., developmental delay, loss of speech and coarse facial features early in childhood. In adulthood, most AGU patients are severely retarded and require special care |
753910 |
| 3.5.1.26 | malfunction |
deficiency of the enzyme causes accumulation of glycoasparagines in lysosomes of cells, resulting in a genetic condition called aspartylglucosaminuria (AGU). AGU is a lysosomal storage disorder caused by defects of the hydrolase glycosylasparaginase. AGU mutations impair autoproteolysis of GA precursor and/or impair its hydrolase activity in lysosomes. This deficiency results in progressive mental decline of the patients, and leads to a lifelong condition affecting patient's appearance, cognition, adaptive skills, physical growth, personality, anatomical structure, and health. Early indicators of AGU include growth spurts in infants and the development of macrocephalia associated to hernias and respiratory infections |
753573 |
| 3.5.1.26 | malfunction |
enzyme point mutation G172D inactivates the enzyme and causes the genetic disease aspartylglucosaminuria, a lysosomal storage disease due to metabolic disorder of lysosomes to digest Asn-linked glycoproteins, structural basis, overview |
735290 |
| 3.5.1.26 | malfunction |
lysosomal acidification inhibitors, chloroquine or bafilomycin A1, disturb medusa morphogenesis at the oral end, suggesting involvement of lysosomal hydrolases in strobilation |
753910 |
