Literature summary for 3.5.1.15 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 .

Search for more literature for 3.5.1.15

Protein Variants

Protein Variants	Comment	Organism
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
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
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
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
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
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
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

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P45381	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
brain	-	Homo sapiens	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
ASPA	-	Homo sapiens

General Information

General Information	Comment	Organism
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

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Release 2023.1 (January 2023)