Date of Award
10-19-2015
Publication Type
Master Thesis
Degree Name
M.Sc.
Department
Chemistry and Biochemistry
Keywords
Computational enzymology, Phosphate cleavage, Quantum mechanics/molecular mechanics, Sulfur intermediates, β-lactamases
Supervisor
Gauld, James
Rights
info:eu-repo/semantics/openAccess
Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial-No Derivative Works 4.0 International License.
Abstract
Enzymes are the bimolecular “workhorses” of the cell due to their range of functions and their requirement for cellular success. The atomistic details of how they function can provide key insights into the fundamentals of catalysis and in turn, provide a blueprint for biotechnological advances. A wide range of contemporary computational techniques has been applied with the aim to characterize recently discovered intermediates or to provide insights into enzymatic mechanisms and inhibition. More specifically, an assessment of methods was conducted to evaluate the presence of the growing number 3– and 4–coordinated sulfur intermediates in proteins/enzymes. Furthermore, two mechanisms have been investigated, the μ-OH mechanism of the hydrolysis of dimethylphosphate in Glycerophosphodiesterase (GpdQ) using five different homonuclear metal combinations Zn(II)/Zn(II), Co(II)/Co(II), Mn(II)/Mn(II), Cd(II)/Cd(II) and Ca(II)/Ca(II) as well as a preliminary study into the effectivness of boron as an inhibitor in the serine protease reaction of class A TEM-1 β-lactamases.
Recommended Citation
Simard, Daniel James, "Computational Investigations on Enzymatic Catalysis and Inhibition" (2015). Electronic Theses and Dissertations. 5440.
https://scholar.uwindsor.ca/etd/5440