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Literature summary extracted from

  • George Priya Doss, C.; Zayed, H.
    Comparative computational assessment of the pathogenicity of mutations in the aspartoacylase enzyme (2017), Metab. Brain Dis., 32, 2105-2118 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.15 E285A the pathogenicity, stability, conservation, change in structural pattern, influence of the mutations on substrate binding of the crystallized mutations (K213E, Y231C, E285A, F295S, I143V and V186D) is compared. Of the crystallized mutations, the mutant E285A is found to be highly conserved as well as affecting the substrate binding with lesser number of overall hydrogen bonds Homo sapiens
3.5.1.15 F295S the pathogenicity, stability, conservation, change in structural pattern, influence of the mutations on substrate binding of the crystallized mutations (K213E, Y231C, E285A, F295S, I143V and V186D) is compared Homo sapiens
3.5.1.15 I143V the pathogenicity, stability, conservation, change in structural pattern, influence of the mutations on substrate binding of the crystallized mutations (K213E, Y231C, E285A, F295S, I143V and V186D) is compared. The binding affinity to the substrate, hydrogen bond interactions and metal interactions are found to be highly disturbed due to the mutant V186D than the mutant I143V Homo sapiens
3.5.1.15 I143V/V186D patients with severe form of Canavan disease (CD) have both missense mutations in the ASPA: c.427 A > G; p. I143V and c.557 T > A; p. V186D. Patient 1 harbors both mutations (p.I143V and p.V186D) in a heterozygous form together with four other mutations, and patient 2 has both mutations in homozygous form Homo sapiens
3.5.1.15 K213E the pathogenicity, stability, conservation, change in structural pattern, influence of the mutations on substrate binding of the crystallized mutations (K213E, Y231C, E285A, F295S, I143V and V186D) is compared. The mutant K213E is found to be least conserved, and the substrate binding affinity is found to be minimal Homo sapiens
3.5.1.15 V186D the pathogenicity, stability, conservation, change in structural pattern, influence of the mutations on substrate binding of the crystallized mutations (K213E, Y231C, E285A, F295S, I143V and V186D) is compared. The binding affinity to the substrate, hydrogen bond interactions and metal interactions are found to be highly disturbed due to the mutant V186D than the mutant I143V. The mutant V186D can be more pathogenic than the mutant I143V Homo sapiens
3.5.1.15 Y231C the pathogenicity, stability, conservation, change in structural pattern, influence of the mutations on substrate binding of the crystallized mutations (K213E, Y231C, E285A, F295S, I143V and V186D) is compared Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.15 Zn2+ zinc-dependent enzyme Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.15 N-acetyl-L-aspartate + H2O Homo sapiens
-
 acetate + L-aspartate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.15 Homo sapiens P45381
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.1.15 brain
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.15 N-acetyl-L-aspartate + H2O
-
 Homo sapiens acetate + L-aspartate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.15 ASPA
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
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 Homo sapiens