EC Number   |
General Information |
Reference |
|---|
   3.5.1.15 | malfunction |
catalytic deficiency of aspartoacylase is associated with several neurodegenerative disorders. The Canavan disease occurs most frequently in Ashkenazi Jews, with more than 96% of cases being associated with two point mutations: Glu285Ala and Tyr231X. The Canavan disease in other ethnic groups is associated with a more diverse range of mutations, the Ala305Glu replacement being the most frequent |
755390 |
| 3.5.1.15 | malfunction |
defects in the ASPA gene that codes for aspartoacylase causes a dramatic elevation in N-acetyl-L-aspartate1 levels, depletion of brain acetate, and leads to demyelination in neuronal cellsenzyme deficiency lead to a loss of activity and the symptoms of a fatal neurological disorder called Canavan disease |
733213 |
| 3.5.1.15 | malfunction |
mutations in gene Aspa lead to Canavan disease characterized by defective synthesis of myelin. Loss of expression of aspartoacylase does not lead to macrophage polarization |
734393 |
| 3.5.1.15 | malfunction |
mutations in the ASPA gene are associated with the development of Canavan disease (CD), leading to the deficiency of ASPA activity. Patients with CD are characterized by degeneration of the white matter of the brain |
754618 |
| 3.5.1.15 | malfunction |
mutations in the ASPA gene cause the Canavan disease, a fatal, childhood neurological disorder leading to catalytic deficiencies in the aspartoacylase (ASPA) enzyme and impaired N-acetyl-l-aspartic acid metabolism in the brain. The mutant enzymes each have overall structures similar to that of the wild-type ASPA enzyme, but with varying degrees of alterations that offer explanations for the respective loss of catalytic activity |
733353 |
| 3.5.1.15 | malfunction |
mutations in the ASPA gene cause the Canavan disease, a fatal, childhood neurological disorder leading to catalytic deficiencies in the aspartoacylase enzyme and impaired N-acetyl-L-aspartic acid metabolism in the brain. Enzyme replacement therapy can potentially be used to overcome these defects if a stable enzyme form that can gain access to the appropriate neural cells can be produced. Achieving the proper cellular targeting requires a modified form of aspartoacylase that can traverse the blood-brain barrier |
734698 |
| 3.5.1.15 | malfunction |
the defect of aspartoacylase is the cause of Canavan disease |
719318 |
| 3.5.1.15 | metabolism |
enzyme substrate N-acetylaspartate is the second-most abundant metabolite in the brain, being produced by neurons and used by oligodendrocytes to coordinate their differentiation, energy production, and lipid synthesis |
734393 |
| 3.5.1.15 | more |
enzyme deficiency is involved in Canavan disease and type 2 diabetes, high levels of N-acetylaspartic acid induce inflammatory agents TNFalpha, p38MAPK, iNOS, PKC, COX2 and ICAM3, and alters proteins levels and smooth muscle contractility, which contributes to the gastrointestinal disorder, overview |
712986 |
| 3.5.1.15 | more |
homology modeling of the N117Q human aspartoacylase mutant using the native structure, PDB ID 2O53, as the template |
733213 |
