Graduation Year


Date of Submission


Document Type

Campus Only Senior Thesis

Degree Name

Bachelor of Arts



Reader 1

Mary Hatcher-Skeers

Reader 2

Bethany Caulkins


Pyridoxal-5’-Phosphate (PLP) enzymes are essential cofactors in many important enzymatic mechanisms. Tryptophan Synthase (TS) is a PLP-dependent enzyme of interest due to its unique kinetics. TS catalyzes the last two steps in the biosynthesis of L-tryptophan from its substrates, serine and indole. The structure of TS is composed of a multienzyme α2β2 complex that contains two functional active sites, the α and β subunits. When higher concentrations of indole are present, it has been shown to exhibit uncompetitive inhibition of TS. Due to the rapid reactivity of indole in this reaction, we are unable to obtain reproducible kinetic data. In this research, we investigate the inhibitory role of indole using a substrate analogue, indoline. Indoline is very similar in structure to indole but has a slower reaction rate. It also creates a novel amino acid when allowed to react with TS. By investigating the kinetics of indoline we can resolve questions about the inhibitory mechanism of indole. In this proposal thesis, we predict that indoline will exhibit uncompetitive inhibition.

This thesis is restricted to the Claremont Colleges current faculty, students, and staff.