ABSTRACT
The urinary excretion of N-acetylaspartic acid was reported by Kvittingen, Hagenfeldt and their colleagues [10,11]. The former reported aspartoacylase activity (Figure 107.1) as normal [10], while the latter correctly documented the deficiency of this enzyme [11]. However, neither group appreciated
that they were dealing with Canavan disease. The association of aspartoacylase deficiency and N-acetyl-aspartic aciduria with Canavan disease was made by Matalon [12] and Divry [13,14] and their colleagues in 1988. Aspartoacylase (EC 3.5.1.15) catalyzes the hydrolysis of N-acetylaspartic acid to l-aspartic and acetic acids (Figure 107.1). Kaul and his colleagues [15-18] cloned the cDNA for aspartoacylase and localized it to the terminal end of the short arm of chromosome 17. They have identified a number of mutations and in the case of the Ashkenazic Jewish population proposed a founder effect in the basis of the predominance of two mutations [19].
