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. DESIGN AND 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. CONCLUSION: Data indicated that this new mutation might be responsible in homozygosis for the phenotype corresponding to Canavan disease.
Tavazzi, B., Di Pietro, V., Amorini, A. M., Giardina, B., Lazzarino, G., A new T677C mutation of the aspartoacylase gene encodes for a protein with no enzymatic activity, <<CLINICAL BIOCHEMISTRY>>, 2008; (41): 611-615 [http://hdl.handle.net/10807/16383]
A new T677C mutation of the aspartoacylase gene encodes for a protein with no enzymatic activity
Tavazzi, Barbara;Di Pietro, Valentina;Amorini, Angela Maria;Giardina, Bruno;Lazzarino, Giuseppe
2008
Abstract
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. DESIGN AND 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. CONCLUSION: Data indicated that this new mutation might be responsible in homozygosis for the phenotype corresponding to Canavan disease.
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
