Bio-Mimicking Pyruvate to Inhibit Lactate Dehydrogenase
- UNCP Author/Contributor (non-UNCP co-authors, if there are any, appear on document)
- Davita Nicole Brockington (Creator)
- Institution
- The University of North Carolina at Pembroke (UNCP )
- Web Site: http://www.uncp.edu/academics/library
- Advisor
- Siva Mandjiny
Abstract: Lactate dehydrogenase is an enzyme that catalyzes the reaction of converting pyruvic acid into lactic acid. This reaction took place at pH 7.0. Molecules, such as acetamide and oxamic acid, which are believed to mimic pyruvate in terms of hydrogen bonding characteristics and ionic interactions with enzymes, were used to mimic pyruvate. Therefore, it is expected that acetamide and oxamic acid will both mimic pyruvate in order to inhibit the activity of lactate dehydrogenase. As expected oxamic acid is a competitive inhibitor of lactate dehydrogenase and acetamide is a noncompetitive inhibitor. The results suggest that the binding of pyruvate to lactate dehydrogenase occurs either at the carboxylic acid functional group and/or the adjacent carbonyl group.
Bio-Mimicking Pyruvate to Inhibit Lactate Dehydrogenase
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Created on 11/29/2012
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Additional Information
- Publication
- Honors Project
- Language: English
- Date: 2012
- Keywords
- Lactate dehydrogenase, Pyruvic acid, Lactic Acid, Mimic Pyruvate, Acetamide, Caboxylic acid functional group, Oxamic acid,