Kenton graduated in 2007 from Harvard University with an A.B. in Chemistry and Anthropology. He spent the next 6 years working in analytical development chemistry at Merck and Company. In 2013, he left Merck and started as a graduate student in Wilfred van der Donk’s lab at the University of Illinois. He is currently working on developing platforms for the directed evolution of lanthipeptides. He hopes to continue on to a postdoc and a career in academia.
Cytolysins CylLL and CylLS are class II lanthipeptides. They are ribosomally synthesized and then post-translationally modified by the bifunctional LanM enzyme CylM. CylM dehydrates select serine and threonine residues to form dehydroalanine or dehydrobutyrine residues. It then catalyzes a Michael-type addition of Cys residues to form thioether linkages. The action of CylM is dependent on the presence of the leader peptide, yet the interacting structural elements of the enzyme and substrates remain unknown. Furthermore, a truncated version of the CylM, which only contains the dehydration domain, is still active, suggesting that there may be multiple binding sites for the substrate. Development via directed evolution of a CylLL variant whose leader more tightly binds either the N-terminal portion or full-length CylM should allow co-crystallization of the enzyme and substrate. Furthermore, characterization of selected library variants will further our understanding of the substrate-enzyme interactions that allow peptide modification.