Literature summary for 3.5.1.15 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.

Protein Variants

Protein Variants	Comment	Organism
A305E	Canavan disease mutation, undetectable enzyme activity	Homo sapiens
A57T	Canavan disease mutation, undetectable enzyme activity	Homo sapiens
C152W	Canavan disease mutation, undetectable enzyme activity	Homo sapiens
D249V	Canavan disease mutation, undetectable enzyme activity	Homo sapiens
D68A	Canavan disease mutation, undetectable enzyme activity	Homo sapiens
E178A	undetectable ASPA activity	Homo sapiens
E214X	Canavan disease mutation, undetectable enzyme activity	Homo sapiens
E24D	putative zinc ion binding sites, undetectable ASPA activity	Homo sapiens
E24G	Canavan disease mutation, undetectable enzyme activity	Homo sapiens
E24G	putative zinc ion binding sites, undetectable ASPA activity	Homo sapiens
E285A	Canavan disease mutation, undetectable enzyme activity	Homo sapiens
F295S	Canavan disease mutation, undetectable enzyme activity	Homo sapiens
G274R	Canavan disease mutation, undetectable enzyme activity	Homo sapiens
H116G	putative zinc ion binding sites, undetectable ASPA activity	Homo sapiens
H21G	putative zinc ion binding sites, undetectable ASPA activity	Homo sapiens
H21P	Canavan disease mutation, undetectable enzyme activity	Homo sapiens
I143T	Canavan disease mutation, undetectable enzyme activity	Homo sapiens
K213E	Canavan disease mutation, undetectable enzyme activity	Homo sapiens
M195R	Canavan disease mutation, undetectable enzyme activity	Homo sapiens
P183H	Canavan disease mutation, undetectable enzyme activity	Homo sapiens
R63N	undetectable ASPA activity	Homo sapiens
R71N	undetectable ASPA activity	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
diisopropyl fluorophosphate	-	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	two zinc ions per enzyme subunit	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
N-acetyl-L-aspartate + H2O	Homo sapiens	enzyme mutations cause the Canavan disease	aspartate + acetate	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P45381	-	-

Purification (Commentary)

Purification (Comment)	Organism
One-step nickel-affinity chromatography	Homo sapiens

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
ASPA	-	Homo sapiens
Aspartoacylase	-	Homo sapiens