Structural and Functional Studies of L-PGDS and SMPDL3A Enzymes in Lipid Signaling Family

This thesis investigated the structure and function of two lipid signaling enzymes, L-PGDS and SMPDL3A, using techniques like X-ray crystallography and NMR spectroscopy. The study revealed that L-PGDS, which produces prostaglandin D2 and acts as a lipophilic ligand carrier, has specific binding sites for substrate catalysis and membrane affinity influenced by the bound ligand. These findings proposed a model for substrate catalysis and product egression, highlighting L-PGDS's dual role in enzymatic activity and transport. Understanding L-PGDS's molecular dynamics could aid in regulating prostaglandin D2 and designing drug delivery systems.