Enzymes are fascinating catalysts from both the point of view of a chemist and that of a biochemist. They can be studied on very different levels, ranging from the “circle meets triangular to produce a square” level, to examination of “arrows pushing” organic mechanisms to the physical chemistry level (dynamics and quantum mechanics). I will demonstrate this range via recent studies of dihydrofolate reductase and thymidylate synthase, which are enzymes catalyzing the <i>de novo</i> biosynthesis of the DNA base T (thymine). The role of such mechanistic understanding in identifying potential targets for antibiotic and chemotherapeutic drugs will be discussed. Aspects of molecular evolution from bacteria to human revealed by those methods will also be discussed.

Enzyme mechanisms: From physical chemistry to evolution and new drug targets

249th National Meeting (2015)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.