Understanding Reductive Enzymes in the Erythritol Biosynthesis Pathway: “The Secrets of Sweet Blood”
| dc.contributor.author | Peyton Lee Carpen | |
| dc.date.accessioned | 2025-03-07T19:16:45Z | |
| dc.date.available | 2025-03-07T19:16:45Z | |
| dc.date.issued | 2023-05-03 | |
| dc.description | Awarded Research Honors | |
| dc.description.abstract | Erythritol is a sugar alcohol and non-nutritive sweetener that the body produces from glucose. Studies have shown a correlation between cardiometabolic dysfunction and increased erythritol production. It is hypothesized that elevated erythritol is a predictive biomarker of cardiometabolic diseases. The overall objectives of this project are to uncover the characteristics of enzymes catalyzing the erythritol biosynthesis pathway through wet lab and computational experiments and to understand how this pathway is causally related to development of cardiometabolic dysfunction. Two human enzymes have been identified as catalyzing the final step in the conversion of glucose to erythritol: ADH1 (alcohol dehydrogenase) & SORD (sorbitol dehydrogenase.) In order to interrogate how these enzymes relate to whole-body cardiometabolic dysfunction, a mouse model is required. The recombinant murine (mouse) ADH1 and SORD enzymes were cloned and purified to discern whether the murine enzymes also catalyze the final step in erythritol production. The enzymatic activity found was comparable between species. However, when mouse models were generated lacking either Adh1 or Sord, there was no robust decrease in erythritol production in mice. These results suggest that enzymes other than ADH1 and SORD catalyze this same activity in mice. Therefore, a computational search was conducted to identify alternative enzymes with structural similarity to ADH1 and SORD that may catalyze this reaction in mice and in humans. ADH5 was one identified as a potential alternate enzyme of interest for future study. | |
| dc.description.sponsorship | Martha Field and Semira Ortiz | |
| dc.identifier.uri | https://hdl.handle.net/1813/116759 | |
| dc.publisher | Cornell Univeristy Press | |
| dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 International | en |
| dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | |
| dc.subject | Diabetes | |
| dc.subject | Erythritol | |
| dc.subject | Cardiometabolic | |
| dc.subject | Sugar Alcohol | |
| dc.subject | ADH1 | |
| dc.subject | SORD | |
| dc.subject | Alcohol Dehydrogenase | |
| dc.subject | Sorbitol Dehydrogenase | |
| dc.subject | Enzyme | |
| dc.subject | Enzymology | |
| dc.subject | Protien Purification | |
| dc.subject | Metabolite | |
| dc.subject | Pentose Phosphate Pathway | |
| dc.subject | Cardiometabolic Disease | |
| dc.subject | Biomarker | |
| dc.subject | Blood Plasma | |
| dc.subject | Enzyme Kinetics | |
| dc.subject | Homology | |
| dc.subject | Computational Biology | |
| dc.subject | Metabolomics | |
| dc.subject | Nutrition | |
| dc.title | Understanding Reductive Enzymes in the Erythritol Biosynthesis Pathway: “The Secrets of Sweet Blood” | |
| dc.type | dissertation or thesis |
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