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Literature summary for 3.4.17.1 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
Search for more literature for 3.4.17.1

Application

Application Comment Organism
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)

Cloned (Comment) Organism
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

Protein Variants Comment Organism
A305E tested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
A57T untested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
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
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
C152W tested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
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
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
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
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
D249V tested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
D68A tested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
E178A mutation of the general proton donor Homo sapiens
E214X tested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
E24D mutation of a putative zinc-binding residue Homo sapiens
E24G mutation of a putative zinc-binding residue, tested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
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
E24H/H116E mutant designed to switch the order of the zinc-binding residues Homo sapiens
E285A tested Canavan Disease mutation Homo sapiens
F295S untested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
G274R untested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
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
H116G mutation of a putative zinc-binding residue Homo sapiens
H21E/E24H mutant designed to switch the order of the zinc-binding residues Homo sapiens
H21G mutation of a putative zinc-binding residue Homo sapiens
H21P untested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
I143T untested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
K213E/G274R untested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
M195R untested Canavan Disease mutation, results in undetectable enzyme activity Homo sapiens
P183H untested Canavan Disease mutation Homo sapiens
R63N mutation that affects transition state stabilization Homo sapiens
R71N mutation that affects substrate carboxyl binding Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+
-
 Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38000
-
 native ASPA expessed in COS-7 cells, determined by immunoblotting Homo sapiens
52000
-
 recombinant human ASPA fused to N-terminal thioredoxin and C-terimal V5 and a 6x-histidine tag, analyzed by SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using nickel affinity chromatography Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-L-aspartate
-
 Homo sapiens acetate + L-aspartate
-
 ?

Synonyms

Synonyms Comment Organism
ASPA
-
 Homo sapiens
aspartoacyclase
-
 Homo sapiens
carboxypeptidase a
-
 Homo sapiens