Aspartoacylase is a key enzyme in the human central nervous system. Catalytic deficiency of aspartoacylase is associated with several neurodegenerative disorders, which accounts for the enhanced interest in description of the catalytic action and regulatory mechanisms of this enzyme. This review focuses on molecular modelling of the catalytic function of aspartoacylase and the ways of its allosteric regulation in terms of modern theoretical chemistry approaches. The conclusions based on experimental data on the structure and functions of aspartoacylase accumulated during the last 20 years and conclusions drawn from computer modelling results of the last 5 years are analyzed in detail. The bibliography includes 109 references.