Speaker
Kai Tittmann
Description
I will present crystallographic snapshots of the human enzyme orotidine-5-monophosphate decarboxylase in complex with the genuine substrate, substrate analogs, transition state analogs and product - all at true atomic resolution. These snapshots of catalysis defy the proposed mechanism of ground-state destabilization by revealing that the substrate carboxylate is protonated and forms a favorable low-barrier hydrogen bond with a negatively charged amino acid.
Primary author
Kai Tittmann
