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Literature summary for 3.5.1.15 extracted from

  • Wijayasinghe, Y.S.; Pavlovsky, A.G.; Viola, R.E.
    Aspartoacylase catalytic deficiency as the cause of Canavan disease: a structural perspective (2014), Biochemistry, 53, 4970-4978.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E285A a naturally occuring missense mutation associated with the Canavan disease, the mutant shows loss of hydrogen bonding interactions with the carboxylate side chain of Glu285, which disturbs the active site architecture leading to altered substrate binding and lower catalytic activity Homo sapiens
F295S a naturally occuring missense mutation associated with the Canavan disease, the mutant shows loss of van der Waals contacts Homo sapiens
K213E a naturally occuring missense mutation associated with a mild phenotype of Canavan disease, a nonconservative mutant, has minimal structural differences compared to the wild-type enzyme Homo sapiens
Y231C a naturally occuring missense mutation associated with the Canavan disease, the mutant shows loss of hydrophobic and hydrogen bonding interactions. The mutation leads to a local collapse of the hydrophobic core structure in the carboxyl-terminal domain, contributing to a decrease in protein stability Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P45381 gene ASPA
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Source Tissue

Source Tissue Comment Organism Textmining
brain
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Homo sapiens
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Synonyms

Synonyms Comment Organism
ASPA
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Homo sapiens

General Information

General Information Comment Organism
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 Homo sapiens