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Literature summary extracted from

  • Zano, S.; Malik, R.; Szucs, S.; Matalon, R.; Viola, R.E.
    Modification of aspartoacylase for potential use in enzyme replacement therapy for the treatment of Canavan disease (2011), Mol. Genet. Metab., 102, 176-180.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
3.5.1.15 medicine mutations in the aspartoacylase aspA gene are implicated as the cause of Canavan Disease Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.15 expressed in Pichia pastoris Homo sapiens

General Stability

EC Number General Stability Organism
3.5.1.15 PEGylated forms of aspartoacylase (modified with PEG of 2 kDa, 5 kDa, 10 kDa, 20 kDa or 40 kDa) show similar activities to that of the native enzyme. The activity of PEGylated enzyme samples is monitored for 72 hours without observing a substantial loss in activity Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.15 35000
-
 x * 35000, SDS-PAGE Homo sapiens

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.15 nickel Sepharose column chromatography and Source 15Q column chromatography 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 L-aspartate + acetate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.15 ? x * 35000, SDS-PAGE Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.5.1.15 ASPA
-
 Homo sapiens