Programmed cell death (PCD), also known as apoptosis, is a critical method in development, reproduction, and responses to stress within the body. Human PCD is mediated by enzymes known as caspases, cysteine proteases which break down other proteins after specific residues in the polypeptide chain. Fungi, plants, and protozoans do not express caspase genes, but rather have homologous proteins known as metacaspases. Because metacaspases are the primary apoptotic enzyme for fungi, studying their proteolytic mechanisms can lead to further research on opportunistic fungal infections and antifungal treatments. There are 3 types of metacaspases categorized accordingly as Type I, Type II, and Type III with varying structure and organization. All three types contain a large p20 catalytic region with a Cys-His catalytic dyad similar to caspases, and a smaller p10 region. The organism used in this research project to understand metacaspase proteolytic function is the basidiomycete fungus Schizophyllum commune (S. commune). My particular research focuses on S. commune Type II metacaspases which are organized with a linker region between p20 and p10 subunits. These proteins are hypothesized to be the chief enzyme in fungal apoptosis, breaking down the linker between the p20 catalytic domain and the p10 regulatory domain. There are six Type II metacaspases that have been identified in the fungus S. commune (labeled ScMCAIIa-f). Type II metacaspases have previously only been studied in the plant Arabadopsis thaliana, making the studies of Type II metacaspases especially crucial. My research project focuses on properly expressing Type IIa metacaspases in E. coli in order to develop an in-depth characterization and compare them to the analyses of Type I metacaspases.