Date of Award
4-1-2022
Document Type
Honors Thesis
Department
Biology
First Advisor
Peter Lyons
Abstract
Carboxypeptidase A1 (CPA1) is an enzyme utilized in digestion. CPA1 contains a prodomain region, which must be cleaved for enzymatic function. The prodomain region has been hypothesized to be necessary for structural stability, as previous studies were unable to produce a functional CPA1 protein without the prodomain region. However, the recent discovery of a related enzyme, Carboxypeptidase 0 (CP0), which does not have a prodomain yet functions enzymatically, challenges this assertion. To determine if the prodomain is essential to the folding of CPA1, an HA-tag was added for detection, and the prodomain was deleted via PCR. A Western blot was performed to determine expression and enzyme assays were conducted to determine function. CPA1 without a prodomain was detected on the Western blot, but did not display activity in the enzyme assays. This indicates that CPA1 without a prodomain folds adequately enough to be expressed but is nonfunctional. Therefore, the prodomain region appears to be necessary for CPA1 structure and functionality.
Recommended Citation
Domecillo, Masy, "The Role of the Prodomain in the Folding of Carboxypeptidase A1" (2022). Honors Theses. 262.
https://digitalcommons.andrews.edu/honors/262
Subject Area
Carboxypeptidases; Enzymes; Digestive enzymes
Creative Commons License
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