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Terpenoids, a class of compounds with 30,000 unique structures, are known to include antitumor compounds, pigments, vitamins, antibiotics, and flavor molecules. Prenyltransferases are the primary enzyme responsible for assembling the carbon backbone of these compounds from five carbon isoprene units. Bioinformatic analysis has indicated that an evolutionary event has resulted in the acquisition of an additional prenyltransferase in Corynebacterium glutamicum (C. glutamicum) compared to the majority of the Corynebacteriaceae. This result suggests that C. glutamicum may produce a non-essential terpenoid compound, or secondary metabolite. Sequencing has confirmed the successful cloning of the aforementioned genes. Present work includes expressing these genes in Escherichia coli, isolating the protein product, and assessing the function in vitro. This data will be used to expand our understanding of the evolutionary path of C. glutamicum compared to other members of the genus. Continuing work will shed light on the function of the third gene for C. glutamicum, and understanding the role of terpenoids in the family Corynebacteriaceae and greater Actinobacteria.

Content Notes

Poster, Final Report Form

First Advisor

Francis Mann



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