Graduation Term
2023
Degree Name
Master of Science (MS)
Department
Department of Chemistry
Committee Chair
Richard Nagorski
Abstract
The Nagorski group’s interest in carbinolamides stems from their role as an intermediate in the mechanism of the peptidylglycine-α-amidating monooxygenase (PAM) enzyme. Various carbinolamide roles have been studied as they pertain to biological processes, but no efforts have been put forth to understand how they react mechanistically. This group has set its focus on the kinetics of the breakdown of various carbinolamide derivatives in aqueous environments. The results gathered have been used to determine the mechanisms by which they break down in different regions of a full pH profile so that light may be shed on how to manipulate them in the enzymatic pathway. This study focuses on the synthesis and kinetic study of both ethyl-2-(benzoylamino)-2-hydroxyacetate and N-[1-hydroxy-2-oxo-2-(ethylamine)ethyl]benzamide derivatives. These neutral compounds were created in order to compare them to the previously studied α-hydroxyhippuric acid charged compound which was discovered to be a substrate for PAM. The mechanisms present in the hydroxide region for the derivatives synthesized in this study will be discussed and then compared to that of α-hydroxyhippuric acid.
Access Type
Thesis-Open Access
Recommended Citation
Kerkemeyer, Elise, "Acyl Derivatives of Α-hydroxyhippuric Acid: Comparison of a Charged Substrate vs a Neutral Substrate for the Aqueous Kinetics" (2023). Theses and Dissertations. 1754.
https://ir.library.illinoisstate.edu/etd/1754
DOI
https://doi.org/10.30707/ETD2023.20231004061829117051.999963