Date of Award
Spring 5-2018
Degree Type
Honors College Thesis
Department
Chemistry and Biochemistry
First Advisor
Douglas Masterson
Advisor Department
Chemistry and Biochemistry
Abstract
Pig Liver Esterase (PLE) is a serine protease enzyme that can interact with one side of a diester to hydrolyze the ester to a carboxylic acid, and research has found that the level of hydrophobicity of side groups can impact the enantioselectivity of PLE hydrolysis.1, 2 The Jones Model is what current researchers use to model the active site of PLE, but the nature of its binding pockets, namely the Hydrophobic Long (HL) pocket, has been called into question.3 Dimethyl 2-((pyrrole-2-yl)methyl)-2-methylmalonate was prepared to be subjected to PLE hydrolysis to see whether enantioselectivity was found. Chiral HPLC revealed 25.32% enantiomeric excess (e.e.) of the diester with the 2-position pyrrole side group. This proves that there are amino acid residues in the HL binding pocket that can interact with a hydrogen bond donor such as pyrrole and gives more credit to the questions of whether the hydrophobic binding pockets of PLE are really so hydrophobic.
Copyright
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Recommended Citation
Long, Brian, "An Exploration of Pyrrole Groups On the Enantioselectivity of Pig Liver Esterase" (2018). Honors Theses. 556.
https://aquila.usm.edu/honors_theses/556