Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Wang, Q.; Viola, R.E.
    Reexamination of aspartoacylase: is this human enzyme really a glycoprotein? (2014), Arch. Biochem. Biophys., 548, 66-73.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.15 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

EC Number Protein Variants Comment Organism
3.5.1.15 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)

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

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.15 Homo sapiens P45381 gene ASPA
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.5.1.15 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)

EC Number Purification (Comment) Organism
3.5.1.15 recombinant His-tagged enzyme from Pichia pastoris strain KM71H by nickel affinity chromatography, dialysis, and anion exchange chromatography Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.1.15 brain
-
 Homo sapiens
-
3.5.1.15 neuronal cell
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.5.1.15 57
-
 recombinant enzyme expressed from Escherichia coli, pH and temperature not specified in the publication Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.15 N-acetylaspartate + H2O
-
 Homo sapiens acetate + L-aspartate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.15 ASPA
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
3.5.1.15 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
3.5.1.15 additional information homology modeling of the N117Q human aspartoacylase mutant using the native structure, PDB ID 2O53, as the template Homo sapiens
3.5.1.15 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