ASPA (aspartoacylase) is a hydrolase enzyme that catalyzes the deacetylation of N-acetylaspartate (NAA) to produce acetate and L-aspartate. This enzymatic activity is particularly important in the brain, where NAA occurs in high concentration and its hydrolysis plays a significant role in maintaining intact white matter. In other tissues, ASPA functions as a scavenger of NAA from body fluids. The enzyme exhibits hydrolase activity acting on carbon-nitrogen bonds in linear amides and ester bonds, with localization in cytoplasmic and nuclear compartments. ASPA mutations cause Canavan disease, a severe leukodystrophy characterized by progressive neurological deterioration due to impaired white matter maintenance. The disease highlights the critical importance of NAA metabolism in central nervous system function. Beyond Canavan disease, ASPA dysfunction has been associated with various conditions including autism spectrum disorders and other abnormalities of metabolism and homeostasis, suggesting NAA metabolism may influence broader neurobiological processes. Given the severe neurological consequences of ASPA deficiency and the blood-brain barrier challenges in treating CNS disorders, gene therapy approaches using adeno-associated virus (AAV) vectors have emerged as promising therapeutic strategies for Canavan disease 123. AAV-mediated ASPA gene replacement could potentially restore enzymatic function and prevent progressive white matter degeneration.