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A new T677C mutation of the aspartoacylase gene encodes for a protein with no enzymatic activity |
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| Authors: | Di Pietro Valentina Gambacurta Alessandra Amorini Angela Maria Finocchiaro Antonino D'Urso Serena Ceccarelli Lia Tavazzi Barbara Giardina Bruno Lazzarino Giuseppe |
| Affiliation: | aInstitute of Biochemistry and Clinical Biochemistry, Catholic University of Rome “Sacro Cuore”, Rome, Italy bDepartment of Experimental Medicine and Biochemical Sciences, University of Rome “Tor Vergata”, Rome, Italy cDepartment of Chemical Sciences, Laboratory of Biochemistry, University of Catania, Viale A. Doria 6, 95125 Catania, Italy |
| Abstract: | ObjectiveTo 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 methodsWild 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.ResultsWhilst kinetic parameters of wild type hASPA were in line with data in literature, I226T-mutated hASPA showed no enzymatic activity.ConclusionData indicated that this new mutation might be responsible in homozygosis for the phenotype corresponding to Canavan disease. |
| Keywords: | Canavan disease N-acetylaspartate N-acetylaspartoacylase T677C mutation Site-directed mutagenesis |
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