The prevention and treatment of malaria is becoming increasingly difficult due to the spread of drug resistance. There is an urgent need for next generation of antimalarials. The M1 and M17 aminopeptidase enzymes represent new drug targets for malaria. Current studies have considered the structure and function of these enzymes but not how they move and how such movement relates to function. The results of this thesis provided fundamental knowledge on how dynamics affects both catalysis and regulation of activity of the two enzymes and provided key information that will be of broad benefit to future drug discovery programs.