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.
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 |