Semester of Graduation
Spring 2026
Degree Type
Thesis
Degree Name
MASTER OF SCIENCE IN CHEMICAL SCIENCES
Department
Department of Chemistry and Biochemistry
Committee Chair/First Advisor
DR. SOON GOO LEE
Second Advisor
DR. MICHAEL VAN DYKE
Third Advisor
DR. ANIMESH ADITYA
Abstract
Eimeria tenella is a causative agent of coccidiosis, one of the most economically damaging parasitic diseases in the poultry industry, and the increasing drug resistance of E. tenella highlights the need for new therapeutic targets for drug development. This study characterizes phosphoethanolamine N-methyltransferase (PMT) from E. tenella (EtPMT), a key enzyme responsible for the biosynthesis of phosphatidylcholine in the phosphobase methylation pathway, as a potential drug target that is highly conserved across apicomplexan parasites. The enzymatic activity of EtPMT was validated by detecting the methylation of phosphoethanolamine to phosphocholine using mass spectrometry, followed by detailed kinetic analyses. Structural analysis using X-ray crystallography determined the apo structure of EtPMT, representing the first apicomplexan PMT structure outside of PMT from Plasmodium. Computational analyses, including molecular docking, identified critical active site residues (Asp138, Tyr170, Tyr185, and Arg189) that interact with the substrate and are conserved in Plasmodium PMTs. Site-directed mutagenesis further confirmed the importance of the active site, as substitution of these essential residues resulted in a loss of enzymatic activity. Overall, these findings establish that EtPMT is a conserved and catalytically significant enzyme and a promising drug target for the development of novel therapeutics against parasitic diseases.