Margaret E. Glasner
professor
Biochemistry and Biophysics
Texas A and M University
United States of America
Biography
Margaret 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.
Research Interest
Evolution of Protein Structure and Function
Publications
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Brizendine, AM, Odokonyero, D, McMillan, AW, Zhu, M, Hull, K, Romo, D et al.. Promiscuity of Exiguobacterium sp. AT1b o-succinylbenzoate synthase illustrates evolutionary transitions in the OSBS family. Biochem. Biophys. Res. Commun. 2014;450 (1):679-84. doi: 10.1016/j.bbrc.2014.06.034. PubMed PMID:24937446. .
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McMillan, AW, Lopez, MS, Zhu, M, Morse, BC, Yeo, IC, Amos, J et al.. Role of an active site loop in the promiscuous activities of Amycolatopsis sp. T-1-60 NSAR/OSBS. Biochemistry. 2014;53 (27):4434-44. doi: 10.1021/bi500573v. PubMed PMID:24955846. .
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Glasner, ME. Finding enzymes in the gut metagenome. Science. 2017;355 (6325):577-578. doi: 10.1126/science.aam7446. PubMed PMID:28183934. .
