Malaria is a serious disease, which annually affects around 300-500 million people and causes 2 million deaths. The disease is caused by Plasmodium parasites with Plasmodium falciparum commonly causing the most serious disease. During the clinical manifestation, the plasmodiidae enter erythrocytes in order to reproduce. Most antimalarial drugs influence the intra-erythrocytic stage of the parasite life-cycle. There is a increasing problem with drug resistance and a constant need of new antimalarial drug targets. In this context, the M17 amino peptidase from P. falciparum 3D7 was investigated as a possible target for new antimalarial drugs due to its crucial role in parasite development. Reducing M17 activity in P.falciparum has shown that the enzyme activity is crucial in the pre-erythrocytic stage of the parasite life-cycle. The functional M17 homo hexamer forms six active sites, which are arranged in a disc like fashion inwards the oligomer. Every active site contains two Zink ions. The X-ray crystal structure of M17 has been solved and a structure-based drug design approach to designing inhibitors of M17 has been undertaken in recent years. Analysis of the X-ray crystal structure showed that a single loop in the M17 monomer (residues 255-273) was flexible and was hypothesized to act as a regulatory mechanism of enzyme activity. This loop may guard the entrance of the active site cavity. Therefore the structure is going to be analyzed by point mutations, cysteine scanning and FRET in order to determine the role of this loop in relation to enzyme activity and substrate processing.