Graduation Year

2020

Document Type

Campus Only Senior Thesis

Degree Name

Bachelor of Arts

Department

Biochemistry

Second Department

French Studies

Reader 1

Emilie Garrigou-Kempton

Reader 2

Mary Hatcher Skeers

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Terms of Use for work posted in Scholarship@Claremont.

Rights Information

© 2020 Kara A Dunne-Dombrink

Abstract

Pyridoxal-5’-Phosphate (PLP) enzymes catalyze numerous metabolic transformations such as racemization, decarboxylation, elimination, and condensation. Tryptophan Synthase (TS) is a PLP enzyme of interest due to its relevance in finding new allosteric inhibitors and its potential role in the treatment of diseases like Tuberculosis (TB). Composed of an a2b2 complex, the subunits of TS interact such that two substrates – indole and serine – metabolize into the essential amino acid L-tryptophan in a β-elimination and replacement reaction catalyzed by PLP. Although the role of indole and serine in the mechanism of TS has been studied, the relationship between the substrate concentrations and reactivity is less understood. Here, we investigate the inhibitory role of indole in tryptophan synthesis, with aims to explore the possible treatment of mycobacterium tuberculosis (Mtb). Through a historical analysis of TB, both globally and in Francophone countries, one can understand the disease’s impact and the present rise in drug resistance. In order to combat this resistance, it is pertinent to find new, nontoxic treatments that can be used with a wide-range of individuals, including vulnerable people with other health conditions. Preliminary UV-Vis results suggest that indole may act as an uncompetitive inhibitor of tryptophan synthesis, which could play a role in drug discovery for Mtb, although further research is needed to confirm this.

Comments

Preliminary Research Study

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