Email address: firstname.lastname@example.org
B.S/B.A. 2008, University of Iowa
Ph.D. 2013, Johns Hopkins University
Postdoctoral fellow at California Institute of Technology, 2013-17
Protein engineering, biocatalysis, enzymology, chemical biology
The chemical diversity of nature is based upon a limited set of metabolites. Simple building blocks, such as amino acids, are transformed into complex natural products that are the basis for many clinically used pharmaceuticals as well as consumer products and diagnostic tools. The Buller lab will develop strategies to widen the chemical space that is accessible to biology by engineering enzymes to functionalize non-natural precursors into useful building blocks.
Our research will advance our understanding of how to engineer new biocatalytic reactions, a major challenge in enzymology. We will contribute to green chemistry by focusing on enzymes that perform challenging chemical reactions in aqueous environments with high selectivity. Interfacing the resultant catalysts with existing metabolic pathways will enable expansion of metabolic pathways to include novel functional groups. Our long-term goals are to use this non-natural metabolism to probe biological systems and to engineer pathways for the sustainable biosynthesis of natural product analogs with altered pharmacologic properties.
Awards and Honors
|Ruth L. Kirschstein NRSA Postdoctoral Fellowship, National Institutes of Health||2015-17|
|Student-Led Climate Assessment Promotes a Healthier Graduate School Environment. Journal of Chemical Education. American Chemical Society; 2020;97:643-650..|
|Modular control ofl-tryptophan isotopic substitutionviaan efficient biosynthetic cascade. Organic & Biomolecular Chemistry. 2020;18:4189-4192..|
|Structure of a bound peptide phosphonate reveals the mechanism of nocardicin bifunctional thioesterase epimerase-hydrolase half-reactions. Nature Communications. 2019;10..|
|Facile in Vitro Biocatalytic Production of Diverse Tryptamines. Chembiochem. 2019;20:1939-1944..|
|Directed Evolution Mimics Allosteric Activation by Stepwise Tuning of the Conformational Ensemble. Journal of the American Chemical Society. 2018;140:7256-7266..|