Graduation Year

2023

Document Type

Campus Only Senior Thesis

Degree Name

Bachelor of Arts

Department

Biology

Reader 1

Bethany Caulkins

Reader 2

Erin Jones

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Terms of Use for work posted in Scholarship@Claremont.

Abstract

Ornithine Decarboxylase (ODC) is a pyridoxal 5′-phosphate (PLP)-dependent enzyme that catalyzes the first step in polyamine synthesis. As its name suggests, ODC catalyzes the decarboxylation of ornithine to putrescine. Since the polyamine pathway is involved in cell proliferation and increases in polyamine concentrations have been linked to carcinogenesis, ODC is a potential therapeutic target for cancer treatment. Additionally, ODC is a known target for sleeping sickness, a fatal disease if untreated that is caused by the parasite Trypanosoma brucei. In mammalian and T. brucei cells, ODC is a homodimer with two active sites that are formed at the dimer interface by residues of both subunits. ODC has a mass of around 50 kDa per subunit: mouse ODC has a mass of 51 kDa per subunit and T. brucei ODC has a mass of 47 kDa per subunit. While the literature on Saccharomyces cerevisiae ODC is not extensive, researchers who determined the nucleotide sequence of the enzyme in the late 1980s found there to be 40% homology between the amino acid residues of S. cerevisiae and mouse ODC in addition to deducing the length and molecular weight of yeast ODC to be nearly identical to that of mouse ODC. Currently no nuclear magnetic resonance (NMR) data for this enzyme exist, which could provide further and more detailed insight into the structure of the S. cerevisiae form. The first step in obtaining this data is to develop a reliable and robust purification procedure for ODC so that enough pure protein can be produced to perform NMR experiments. While a purification procedure for S. cerevisiae ODC is still being optimized, SDS-PAGE results show the protein to have a mass of around 50 kDa in its monomer form and 100 kDa in its dimer form.

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