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Literature summary for 3.5.1.15 extracted from
- Reexamination of aspartoacylase: is this human enzyme really a glycoprotein? (2014), Arch. Biochem. Biophys., 548, 66-73.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene acy2 or ASPA, recombinant expression of His-tagged enzyme in Pichia pastoris strain KM71H and in Escherichia coli. Recombinantly-expressed human aspartoacylase is not glycosylated, but is still fully functional and stable even when produced from a bacterial expression system | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| N117Q | homology modeling of the N117Q human aspartoacylase mutant using the native structure, PDB ID 2O53, as the template | Homo sapiens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| N-acetylaspartate + H2O | Homo sapiens | - |
acetate + L-aspartate | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P45381 | gene ASPA | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | presence of a glycan at Asn117 that plays an essential role in the stability and catalytic activity of mammalian aspartoacylase. Although recombinantly-expressed human aspartoacylase is not glycosylated, mass spectrometric analysis, overview. The recombinant enzyme is still fully functional and stable, even when produced from a bacterial expression system | Homo sapiens |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Pichia pastoris strain KM71H by nickel affinity chromatography, dialysis, and anion exchange chromatography | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| brain | - |
Homo sapiens | - |
| neuronal cell | - |
Homo sapiens | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 57 | - |
recombinant enzyme expressed from Escherichia coli, pH and temperature not specified in the publication | Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| N-acetylaspartate + H2O | - |
Homo sapiens | acetate + L-aspartate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ASPA | - |
Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | defects in the ASPA gene that codes for aspartoacylase causes a dramatic elevation in N-acetyl-L-aspartate1 levels, depletion of brain acetate, and leads to demyelination in neuronal cellsenzyme deficiency lead to a loss of activity and the symptoms of a fatal neurological disorder called Canavan disease | Homo sapiens |
| additional information | homology modeling of the N117Q human aspartoacylase mutant using the native structure, PDB ID 2O53, as the template | Homo sapiens |
| physiological function | aspartoacylase catalyzes the selective breakdown of N-acetyl-L-aspartate to release acetate in the brain. The acetate provides the building blocks required for fatty acid biosynthesis | Homo sapiens |
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Release 2023.1 (January 2023)
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