Primary Submission Contact

Zachary Bennett

Faculty Sponsor

David Sherman

Faculty Sponsor Email Address


Arts and Sciences



Document Type

Poster Presentation


Fall 10-25-2019


Malbrancheamide is a fungal natural product with significant vasorelaxation effects and potential as a cardiovascular therapeutic. The dichlorination of the indole ring is key for its biological activity, and this transformation is performed by the flavin dependent halogenase MalA. This enzyme utilizes a proposed chloramine lysine intermediate to iteratively and selectively chlorinate its natural substrate premalbrancheamide. Halogenases can provide orthogonal selectivity to many chemical methods, making them useful for pharmaceutical applications, while providing selective methods for late-stage functionalization. This investigation focuses on the substrate scope of the halogenase on complex pharmaceutically relevant substrates in collaboration with the Novartis Institutes for Biomedical Research. The bromination and chlorination reaction conditions were optimized, and the products were structurally characterized by NMR spectroscopy to gain further understanding of the versatility of the wild type enzyme and its mutants.

Biographical Information about Author(s)

I got the opportunity to do research at the University of Michigan over the summer through the Centers for Carbon to Hydrogen Functionalization summer research program. As a biochemistry major, I'm interested in enzymes and their functions and applications. Dr. Sherman's lab determines the pathways that bacteria and fungi use to create bioactive molecules, and the enzymes that produce them. I love being able to look at the mechanisms of these proteins and being able to use them for applications such as drug development.

Additional Presentation Information

Wall Poster