The enzyme adenylosuccinate lyase (ASL) plays a critical role in both cellular metabolism, in particular DNA replication, via its action in the de novo purine biosynthetic pathway. Adenylosuccinate lyase is the only enzyme in this pathway to catalyze two separate reactions, enabling it to participate in the addition of a nitrogen at two different positions in adenosine monophosphate. Because adenylosuccinate lyase plays an integral part in maintaining proper cellular metabolism, mutations in the human enzyme can have severe clinical consequences, including mental retardation with autistic features. Several point mutations in ASL have been identified that are associated with deficiency of enzymatic activity and either psychomotor retardation or autistic features. Six of them were performed and had their kinetic parameters established. Considering its relevance, the purpose of this study is to associate these point mutations with the kinetic properties trough the structural modification. After validation of a 3D structure of human the ASL by molecular modeling techniques, these six point mutations were structurally evaluated and compared to their kinetic values. This analysis will bring new insights into the understanding of structural mutations and ASL activity.