A conserved aspartate of RNA pseudouridine synthase is essential for activity and a probable nucleophilic catalyst

Research was conducted to investigate the mechanisms of pseudouridine synthases, an enzyme which transforms uridine to pseudouridine in a number of positions. Plasmid pLX1 was turned into BL21(DE3) cells while reaction mixtures were incubated in a buffer. Results showed that the target uracil remained bounded to the enzyme until product formation. They also indicated the importance of fluorouracil in covalent complex formation via 39 target positions.