Human Pepsin 3A (1QRP) is an aspartyl protease secreted by the gastric mucosa of the stomach and is necessary for initial protein digestion. The two aspartic acid residues in the active site facilitate hydrolytic catalysis. A previous study refined the crystal structure of 1QRP and its phosphonate inhibitor. In this study, we used MOPAC2012 to calculate the heat of formation of the enzyme-inhibitor complex in order to determine the lowest energy structure. We then examined 1QRP with its substrate peptide to find the most energetically favorable transitions states and ultimately the reaction mechanism.

Human pepsin 3A hydrolysis reaction mechanism

249th National Meeting (2015)

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