A new T677C mutation of the aspartoacylase gene encodes for a protein with no enzymatic activity.
OBJECTIVE
To verify the effect of and to date the unknown T677C mutation of the human N-acetylaspartoacylase (hASPA) gene on the function of the mutated enzyme.


METHODS
Wild type and I226T-mutated proteins were expressed and purified from a transformed Escherichia coli colony. Enzymatic activities were measured in the presence of varying substrate concentrations.


RESULTS
Whilst kinetic parameters of wild type hASPA were in line with data in literature, I226T-mutated hASPA showed no enzymatic activity.


CONCLUSIONS
Data indicated that this new mutation might be responsible in homozygosis for the phenotype corresponding to Canavan disease.
Di Pietro
Valentina
V
Institute of Biochemistry and Clinical Biochemistry, Catholic University of Rome Sacro Cuore, Rome, Italy.
Gambacurta
Alessandra
A
Amorini
Angela Maria
AM
Finocchiaro
Antonino
A
D'Urso
Serena
S
Ceccarelli
Lia
L
Tavazzi
Barbara
B
Giardina
Bruno
B
Lazzarino
Giuseppe
G
D000581:Amidohydrolases / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification; D019943:Amino Acid Substitution / Q000235:genetics; D017825:Canavan Disease / Q000175:diagnosis / Q000201:enzymology / Q000235:genetics; D002675:Child, Preschool; D003596:Cytosine; D004789:Enzyme Activation / Q000235:genetics; D005260:Female; D006801:Humans; D008297:Male; D016297:Mutagenesis, Site-Directed; D009154:Mutation / Q000235:genetics*; D013941:Thymine
D003596:Cytosine; D000581:Amidohydrolases; C019751:aspartoacylase; D013941:Thymine