Glasner, Margaret individual record
Associate Professor
overview

Evolution is the organizing principle of biology and provides the cornerstone of our approach to understand the relationships between protein structure and function. We combine bioinformatics, biochemistry, and genetics to address fundamental questions about protein evolution, such as: What structural and mechanistic features of enzymes increase their capacity to evolve new functions? How do new metabolic pathways evolve? Are there multiple evolutionary pathways to evolve new enzyme activities?



Our primary focus is on how catalytic promiscuity serves as the raw material for evolving new enzyme activities. Catalytic promiscuity is the ability to catalyze different chemical reactions using the same active site. Many enzymes in one branch of the protein family we are studying are catalytically promiscuous, and this activity has been incorporated into new metabolic pathways more than once. Comparing the sequences and structures of these proteins will identify characteristics that permitted them to evolve the second activity.



Our goal is to use results from our research to identify fundamental evolutionary principles that can can help decipher protein structure-function relationships, predict protein functions, and improve protein engineering methods.

selected publications
Academic Articles25
  • Truong, D. P., Rousseau, S., Machala, B. W., Huddleston, J. P., Zhu, M., Hull, K. G., ... Glasner, M. E. (2021). Second-Shell Amino Acid R266 Helps Determine N-Succinylamino Acid Racemase Reaction Specificity in Promiscuous N-Succinylamino Acid Racemase/o-Succinylbenzoate Synthase Enzymes. Biochemistry. (50), 3840.
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  • Glasner, M. E., Truong, D. P., & Morse, B. C. (2020). How enzyme promiscuity and horizontal gene transfer contribute to metabolic innovation. 287(7), 1323-1342.
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  • Burroughs, A. M., Glasner, M. E., Barry, K. P., Taylor, E. A., & Aravind, L. (2019). Oxidative opening of the aromatic ring: Tracing the natural history of a large superfamily of dioxygenase domains and their relatives. 294(26), 10211-10235.
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  • Odokonyero, D., McMillan, A. W., Ramagopal, U. A., Toro, R., Truong, D. P., Zhu, M., ... Glasner, M. E. (2018). Comparison of Alicyclobacillus acidocaldarius o-Succinylbenzoate Synthase to Its Promiscuous N-Succinylamino Acid Racemase/ o-Succinylbenzoate Synthase Relatives.. Biochemistry. (26), 3689.
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  • Glasner, M. E. (2017). Finding enzymes in the gut metagenome. 355(6325), 577-578.
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Books1
  • Glasner, M. E., Gerlt, J. A., & Babbitt, P. C. (2007). Mechanisms of protein evolution and their application to protein engineering.
Conference Papers3
  • McMillan, A., Odokonyero, D., Lopez, M., Woodard, D., Brizendine, A., & Glasner, M. E. (2014). Evolutionary Exploitation of Promiscuous NSAR/OSBS Enzymes. 23, 252-252.
  • Kalyanaraman, C., Glasner, M. E., Chiang, R., Fayazmanesh, N., Babbitt, P., & Jacobson, M. P. (2006). Ligand based clustering of alpha-beta barrel enzymes. 232, 10-10.
  • Glasner, M. E., Fayazmanesh, N., Chiang, R., Jacobson, M. P., Gerlt, J. A., & Babbitt, P. C. (2006). Evolution of structure and function in the o succinylbenzoate synthase family. The FASEB Journal. 20(5), a905-a905.
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chaired theses and dissertations
Email
margy.glasner@tamu.edu
First Name
Margaret
Last Name
Glasner
mailing address
Texas A&M University; Biochemistry & Biophysics; 2128 TAMU
College Station, TX 77843-2128
USA