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Literature summary extracted from

  • Hershfield, J.R.; Pattabiraman, N.; Madhavarao, C.N.; Namboodiri, M.A.
    Mutational analysis of aspartoacylase: implications for Canavan disease (2007), Brain Res., 1148, 1-14.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
3.4.17.1 medicine mutations that results in near undetectable activity of aspartocyclase correlate with Canavan Disease, a neurodegenerative disorder usually fatal during childhood Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.17.1 full-length human ASPA cDNA is subcloned into the pcDNA3.1/V5-His-TOPO vector, for bacterial expression mutants are generated directly in the pBAD/Thio-TOPO vector Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.4.17.1 A305E tested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
3.4.17.1 A57T untested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
3.4.17.1 C124A alanine substitution of Cys124, residue indicates by homology modelling to be in close proximity and in the proper orientation for disufide bonding Homo sapiens
3.4.17.1 C152A alanine substitution of Cys152, residue indicates by homology modelling to be in close proximity and in the proper orientation for disufide bonding Homo sapiens
3.4.17.1 C152W tested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
3.4.17.1 C61A mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme Homo sapiens
3.4.17.1 C61S mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme Homo sapiens
3.4.17.1 C61W mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme Homo sapiens
3.4.17.1 D204H mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme Homo sapiens
3.4.17.1 D249V tested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
3.4.17.1 D68A tested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
3.4.17.1 E178A mutation of the general proton donor Homo sapiens
3.4.17.1 E214X tested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
3.4.17.1 E24D mutation of a putative zinc-binding residue Homo sapiens
3.4.17.1 E24G mutation of a putative zinc-binding residue, tested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
3.4.17.1 E24H mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme Homo sapiens
3.4.17.1 E24H/H116E mutant designed to switch the order of the zinc-binding residues Homo sapiens
3.4.17.1 E285A tested Canavan Disease mutation Homo sapiens
3.4.17.1 F295S untested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
3.4.17.1 G274R untested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
3.4.17.1 H116E mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme Homo sapiens
3.4.17.1 H116G mutation of a putative zinc-binding residue Homo sapiens
3.4.17.1 H21E/E24H mutant designed to switch the order of the zinc-binding residues Homo sapiens
3.4.17.1 H21G mutation of a putative zinc-binding residue Homo sapiens
3.4.17.1 H21P untested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
3.4.17.1 I143T untested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
3.4.17.1 K213E/G274R untested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
3.4.17.1 M195R untested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
3.4.17.1 P183H untested Canavan Disease mutation Homo sapiens
3.4.17.1 R63N mutation that affects transition state stabilization Homo sapiens
3.4.17.1 R71N mutation that affects substrate carboxyl binding Homo sapiens
3.5.1.15 A305E Canavan disease mutation, undetectable enzyme activity Homo sapiens
3.5.1.15 A57T Canavan disease mutation, undetectable enzyme activity Homo sapiens
3.5.1.15 C152W Canavan disease mutation, undetectable enzyme activity Homo sapiens
3.5.1.15 D249V Canavan disease mutation, undetectable enzyme activity Homo sapiens
3.5.1.15 D68A Canavan disease mutation, undetectable enzyme activity Homo sapiens
3.5.1.15 E178A undetectable ASPA activity Homo sapiens
3.5.1.15 E214X Canavan disease mutation, undetectable enzyme activity Homo sapiens
3.5.1.15 E24D putative zinc ion binding sites, undetectable ASPA activity Homo sapiens
3.5.1.15 E24G Canavan disease mutation, undetectable enzyme activity Homo sapiens
3.5.1.15 E24G putative zinc ion binding sites, undetectable ASPA activity Homo sapiens
3.5.1.15 E285A Canavan disease mutation, undetectable enzyme activity Homo sapiens
3.5.1.15 F295S Canavan disease mutation, undetectable enzyme activity Homo sapiens
3.5.1.15 G274R Canavan disease mutation, undetectable enzyme activity Homo sapiens
3.5.1.15 H116G putative zinc ion binding sites, undetectable ASPA activity Homo sapiens
3.5.1.15 H21G putative zinc ion binding sites, undetectable ASPA activity Homo sapiens
3.5.1.15 H21P Canavan disease mutation, undetectable enzyme activity Homo sapiens
3.5.1.15 I143T Canavan disease mutation, undetectable enzyme activity Homo sapiens
3.5.1.15 K213E Canavan disease mutation, undetectable enzyme activity Homo sapiens
3.5.1.15 M195R Canavan disease mutation, undetectable enzyme activity Homo sapiens
3.5.1.15 P183H Canavan disease mutation, undetectable enzyme activity Homo sapiens
3.5.1.15 R63N undetectable ASPA activity Homo sapiens
3.5.1.15 R71N undetectable ASPA activity Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.15 diisopropyl fluorophosphate
-
 Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.17.1 Zn2+
-
 Homo sapiens
3.5.1.15 Zn2+ two zinc ions per enzyme subunit Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.17.1 38000
-
 native ASPA expessed in COS-7 cells, determined by immunoblotting Homo sapiens
3.4.17.1 52000
-
 recombinant human ASPA fused to N-terminal thioredoxin and C-terimal V5 and a 6x-histidine tag, analyzed by SDS-PAGE 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-acetyl-L-aspartate + H2O Homo sapiens enzyme mutations cause the Canavan disease aspartate + acetate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.17.1 Homo sapiens
-
-
-
3.5.1.15 Homo sapiens P45381
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.17.1 using nickel affinity chromatography Homo sapiens
3.5.1.15 One-step nickel-affinity chromatography Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.17.1 N-acetyl-L-aspartate
-
 Homo sapiens acetate + L-aspartate
-
 ?
3.5.1.15 N-acetyl-L-aspartate + H2O enzyme mutations cause the Canavan disease Homo sapiens aspartate + acetate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.17.1 ASPA
-
 Homo sapiens
3.4.17.1 aspartoacyclase
-
 Homo sapiens
3.4.17.1 carboxypeptidase a
-
 Homo sapiens
3.5.1.15 ASPA
-
 Homo sapiens
3.5.1.15 Aspartoacylase
-
 Homo sapiens