Education
- Ph.D., in Pharmaceutical Sciences, University of Texas at Austin
- B.S., in Chemistry, Kentucky State University
- B.S., in Biology, Kentucky State University
Courses
- Biochemistry
- General Biology
- General Chemistry
- Cell and Molecular Methods
Biography
Emily Lancaster was born and raised in central Kentucky. She attended the Historically Black College/University (HBCU) Kentucky State University between 2011-2015, earning two Bachelor of Science degrees in Chemistry and Biology. She then moved to Austin, Texas to study and earn her Ph.D. in Pharmaceutical Sciences with a concentration in Chemical Biology and Medicinal Chemistry. The focus of her graduate work centered around learning how enzymes worked. One enzyme was trans-o-hydroxybenzylidinepyruvate hyratase-aldolase (NahE), a member of the Aldolase Superfamily involved in the pathway of enzymes belonging to a bacteria that degrades polycyclic aromatic hydrocarbons (PAHs). The second set of enzymes came from the Tautomerase Superfamily, wherein a bioinformatic approach was used to visualize the relationship between an enzyme’s sequence and its function across more than 50,000 sequences predicted to do up to 7 different types of chemistries.
After defending her dissertation in 2022, she moved to San Antonio, TX as an IRACDA-SABER postdoctoral scholar. The IRACDA program served as a platform to conduct traditional postdoctoral research training and to acquire more training on teaching practices in the undergraduate classroom, as Lancaster knew early in graduate school that she wanted to serve as an instructor for fledgling scientists at the undergraduate level. Her postdoctoral research focused on the connection between transcriptional stress and the intrinsically disordered EWS region of the fused protein EWS-FLI1, which is attributed to 85% of Ewing Sarcoma cases in young adults and children.
Lancaster brings both of these big projects to St. Mary’s as research projects for undergraduates in her lab, both anchored in enzymatic techniques. When she is not in the lab or classroom, Lancaster tends to her many houseplants in her office, attempts to grow a variety of flowers and vegetables in her garden at home, plans the next home-improvement project and plays string with her many kitties.
Publications
Lancaster, E.B., Haley A. Hardtke , Trevor R. Melkonian, Mukesh K. Venkat Ramani, William H. Johnson, Jr, Bert-Jan Baas, Y. Jessie Zhang, and Christian P. Whitman. (2025) Conversion of Inactive Non-Pro1. Tautomerase Superfamily Members into Active Tautomerases: Analysis of the Pro1 Mutants. Biochemistry.
Lancaster, E.B., Yang, W., Johnson, W.H., Baas, B.J., Zhang, Y.J., Whitman, C.P. Kinetic Characterization and Inhibition of Non-Pro1 Malonate Semialdehyde Decarboxylases. Manuscript in progress.
Lancaster, E.B., Johnson, W.H., LeVieux, J.A., Whitman, C.P. (2023) A Mutagenic Analysis of NahE, a Hydratase-Aldolase in the Naphthalene Degradative Pathway. Arch Biochem Biophys. 733:109471.
Sipe, S., Lancaster, E.B., Butalewicz, J., Whitman, C.P., Brodbelt, J. (2022) Symmetry of 4-Oxalocrotonate Tautomerase Trimers Influences Unfolding and Fragmentation in the Gas Phase. J. Am. Chem. Soc. 144(27):12299-12309.
Lancaster, E.B., Yang, W., Johnson, W.H., Baas, B.J., Zhang, Y.J., Whitman, C.P. (2022) Kinetic, Inhibition, and Structural Characterization of a Malonate Semialdehyde Decarboxylase-like Protein from Calothrix sp. PCC 6303: A Gateway to the non-Pro1 Tautomerase Superfamily Members. Biochemistry. 10.1021/acs.biochem2c00101.
Baas, B.J., Medellin, B.P., LeVieux J.A., Erwin, K.L., Lancaster, E.B., Kaoud, T.S., Moreno, Y.R., Babbitt, P.C., Zhang, Y.J., and Whitman, C.P. (2021) Kinetic and Structural Analysis of Two Linkers in the Tautomerase Superfamily: Analysis and Implications. Biochemistry. 60(22), 1776-1786.
Medellin, B.P., Lancaster, E.B., Brown, S.D., Rakhade, S., Babbit, P.C., Whitman, C.P., Zhang, Y.J. (2020). Structural Basis for the Asymmetry of a 4-Oxalocrotonate Tautomerase Trimer. Biochemistry. 59, 1592-1603.