3.5.1.15: aspartoacylase
This is an abbreviated version!
For detailed information about aspartoacylase, go to the full flat file.
Word Map on EC 3.5.1.15
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3.5.1.15
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canavan
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n-acetylaspartate
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leukodystrophy
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matter
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myelin
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oligodendrocyte
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spongy
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n-acetyl-l-aspartate
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spongiform
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macrocephaly
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tremor
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ashkenazi
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jewish
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non-jewish
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dysmyelination
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nutrition
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medicine
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pharmacology
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n-acetylaspartylglutamate
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triacetate
- 3.5.1.15
- canavan
- n-acetylaspartate
- leukodystrophy
- matter
- myelin
- oligodendrocyte
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spongy
- n-acetyl-l-aspartate
-
spongiform
- macrocephaly
- tremor
-
ashkenazi
-
jewish
-
non-jewish
-
dysmyelination
- nutrition
- medicine
- pharmacology
- n-acetylaspartylglutamate
- triacetate
Reaction
Synonyms
acetyl-aspartic deaminase, Acylase II, aminoacylase 2, Aminoacylase II, aminoacylase-2, ASPA, aspartic acid acylase, Aspartoacylase, aspartoacylase II, hASPA, human ASPA, More, murine aspartoacylase, N-acetyl-aspartate deacetylase, N-Acetyl-L-aspartate amidohydrolase, N-Acetylaspartate amidohydrolase, N-acetylaspartocylase, NAA acylase
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General Information
General Information on EC 3.5.1.15 - aspartoacylase
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malfunction
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
physiological function
additional information
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
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
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
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
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
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
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aspartoacylase activity supports adenosine triphosphate synthesis in oligodendrocytes during hypoglycemia in vitro. The loss of enzyme function during the early stages of postnatal development significantly compromises oligodendrocyte oxidative integrity
physiological function
Aspa might be relevant to the loss of viable macrophages in the peritoneum, transcription factor Gata6 regulates aspartoacylase expression in resident peritoneal macrophages and controls their survival, perturbed metabolic regulator aspartoacylase facilitates generation of acetyl CoA, gene expression profiling and phenotype, overview. Mutant mice lacking functional Aspa phenocopy the higher propensity to death leading to a contraction of resident peritoneal macrophages
physiological function
aspartoacylase catalyzes the selective breakdown of N-acetyl-L-aspartate to release acetate in the brain. The acetate provides the building blocks required for fatty acid biosynthesis
physiological function
aspartoacylase is a key enzyme in the human central nervous system
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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
additional information
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lack of aspartoacylase activity disrupts survival and differentiation of neural progenitors and oligodendrocytes in a mouse model of Canavan disease. ASPA knockout leads to degeneration of white matter
additional information
homology modeling of the N117Q human aspartoacylase mutant using the native structure, PDB ID 2O53, as the template
additional information
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homology modeling of the N117Q human aspartoacylase mutant using the native structure, PDB ID 2O53, as the template