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dc.contributor.authorParviainen, Anna
dc.date.accessioned2023-08-03T18:36:45Z
dc.date.available2023-08-03T18:36:45Z
dc.date.issued2023-05
dc.identifier.urihttp://hdl.handle.net/10675.2/624727
dc.descriptionThe file you are attempting to access is restricted to Augusta University. Please login using your JagNet iD and password.en_US
dc.description.abstractNatural products (NPs) are nonessential metabolites produced by organisms that are often used in the production of pharmaceuticals. Their natural purpose is to protect their producing organism from the environment, making them an attractive medium for the starting point of drug discovery. NPs are generally very diverse in structure and therefore difficult to reproduce or alter structurally using organic synthesis. Understanding how NPs are synthesized in Nature aids researchers in developing new tools to produce novel NP-like bioactive compounds. The enzymatic pathway this project investigates is a homologation pathway found in the cyanobacterium Nostoc punctiforme PCC 73102 that serves to add a methylene (-CH2-) group to the side chain of an amino acid. Characterization of enzymes in this pathway could lead to the ability to artificially homologate other natural products, a tool that would be valuable because the addition of a methylene group has been shown to improve the biological activity of compounds. The two enzymes involved in this pathway that are being investigated in this project are dehydrogenase/decarboxylase HphB and an aromatic aminotransferase (ArAT). The goal of this project is to clone, express, and purify these enzymes and then test their enzymatic activity to characterize their detailed functions. The two enzymes of interest have been successfully purified by the biochemical technique affinity column chromatography, and the activity of ArAT is currently being investigated by applying the analytical method high performance liquid chromatography (HPLC) to experimental assays. The knowledge gained from this project will shed light on an unknown enzymatic pathway, which could ultimately lead to the development of a new enzymatic tool.
dc.language.isoen_USen_US
dc.publisherAugusta Universityen_US
dc.rightsCopyright protected. Unauthorized reproduction or use beyond the exceptions granted by the Fair Use clause of U.S. Copyright law may violate federal law.en_US
dc.titleInvestigation of HphB and an ArAT in a Homologation Pathway Department of Chemistry & Physicsen_US
dc.typeThesisen_US
dc.contributor.departmentChemistryen_US
dc.description.advisorShogo Mori
dc.description.committeeBo bby Ba r ker
dc.description.committeeBrian Armstrong
dc.description.embargo5/01/2028


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