Researchers from the Emil Pai Lab in collaboration with the Miller Lab (Depts. of Chemistry and Physics, University of Toronto) have pieced together a time-lapse movie revealing all the major steps during the catalytic cycle of an enzyme. This study, published in Science, is the most detailed depiction of such a process to date.
The communication between the protein units is accomplished via a water-network somewhat akin to a […]
The crystal structure of ClpP protease activated by the experimental Phase 2 anti-cancer drug ONC 201, as determined by graduate student Ondrej Halgas in Emil F. Pai’s lab, was featured on the cover of the current issue (May 13th, 2019) of the journal Cancer Cell. Together with the laboratories of Walid Houry, Aaron Schimmer (Medical Biophysics) and Michael Andreeff (MD Anderson, Texas), they identified ClpP as the […]
Researchers in Prosser Lab and Pai Lab recently published in Science on the Role of Dimer Asymmetry and Protomer Dynamics in Enzyme Catalysis.
The associated YouTube video can be viewed here.
The dimeric enzyme fluoroacetate dehalogenase is one of only a handful of protein catalysts that can break the strongest bond in organic chemistry, the one between carbon and fluorine atoms, in the process transforming the highly toxic pesticide fluoroacetate into glycolate, a benign molecule. The laboratories of Emil Pai and Scott Prosser, together with the group of Régis Pomès and collaborators in the US and Japan, have […]