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Literature summary for 3.5.1.15 extracted from

  • Herga, S.; Berrin, J.G.; Perrier, J.; Puigserver, A.; Giardina, T.
    Identification of the zinc binding ligands and the catalytic residue in human aspartoacylase, an enzyme involved in Canavan disease (2006), FEBS Lett., 580, 5899-5904.
    View publication on PubMed
Search for more literature for 3.5.1.15

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes as GST-fusion proteins in Escherichia coli strain BL21(DE3) Homo sapiens

Protein Variants

Protein Variants Comment Organism
E178D site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme Homo sapiens
E178Q site-directed mutagenesis, inactive mutant Homo sapiens
E24A site-directed mutagenesis, inactive mutant Homo sapiens
H116A site-directed mutagenesis, inactive mutant Homo sapiens
H21A site-directed mutagenesis, inactive mutant Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.2
-
 N-acetylaspartic acid pH 7.4, 37°C, recombinant wild-type enzyme Homo sapiens
0.22
-
 N-acetylaspartic acid pH 7.4, 37°C, recombinant mutant E178D Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ metallopeptidase, the enzyme contains the conserved H21XXE24(91aa)H116 motif, ligand binding by His21, Glu24, and His116, molecular modeling Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36000
-
 x * 36000, recombinant enzyme, SDS-PAGE Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-acetylaspartic acid + H2O Homo sapiens enzyme deficiency causes the Canavan disease, an autosomal-recessive neurodegenerative disorder L-asparatate + acetate
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant GST-fusion enzymes from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
N-acyl-L-aspartate + H2O = a carboxylate + L-aspartate reaction mechanism involving Glu178, molecular modeling Homo sapiens
a

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
300
-
 purified recombinant mutant E178D Homo sapiens
1557
-
 purified recombinant wild-type enzyme Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetylaspartic acid + H2O
-
 Homo sapiens L-asparatate + acetate
-
 ?
N-acetylaspartic acid + H2O enzyme deficiency causes the Canavan disease, an autosomal-recessive neurodegenerative disorder Homo sapiens L-asparatate + acetate
-
 ?

Subunits

Subunits Comment Organism
? x * 36000, recombinant enzyme, SDS-PAGE Homo sapiens
More the enzyme belongs to the carboxypeptidase metalloprotein family with the conserved H21XXE24(91aa)H116 motif Homo sapiens

Synonyms

Synonyms Comment Organism
ASPA
-
 Homo sapiens
More the enzyme belongs to the carboxypeptidase metalloprotein family Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.52
-
 N-acetylaspartic acid pH 7.4, 37°C, recombinant wild-type enzyme Homo sapiens
1.48
-
 N-acetylaspartic acid pH 7.4, 37°C, recombinant mutant E178D Homo sapiens
14.22
-
 N-acetylaspartic acid pH 7.4, 37°C, recombinant wild-type enzyme Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Homo sapiens