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dc.contributor.advisorTanner, John J., 1961-eng
dc.contributor.authorWhite, Tommi Annaeng
dc.date.issued2007eng
dc.date.submitted2007 Springeng
dc.descriptionThe entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file.eng
dc.descriptionTitle from title screen of research.pdf file (viewed on March 24, 2009)eng
dc.descriptionVita.eng
dc.descriptionThesis (Ph.D.) University of Missouri-Columbia 2007.eng
dc.description.abstractCatabolism is the oxidation of organic nutrients into simple end molecules to extract energy. For proline, the catabolic pathway involves two enzymes, Lproline dehydrogenase (PRODH, EC 1.5.99.8) and L-[delta]¹-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC 1.5.1.12). Via the action of PRODH and P5CDH, proline can be utilized both as a carbon and nitrogen source. The conventional view of proline catabolism was that PRODH and P5CDH appear as separate enzymes in eukaryotes and as fused bifunctional enzymes (PutA) in bacteria. Analysis of genome sequence data, however, revealed a more complex situation for bacteria. The updated view is that PutAs are indeed restricted to bacteria, but monofunctional PRODHs and P5CDHs appear in both eukaryotes and bacteria. One of these newly discovered bacterial monofunctional PRODHs was chosen and characterized. This work resulted in kinetic and structural analysis of PRODH from Thermus thermophilus. T. thermophilus PRODH was also used for studying mechanism-based inactivation by N-propargylglycine. This work has also resulted in the first structure of a covalently modified PRODH as well as characterization of inactivation kinetics. Physical and functional interactions between monofunctional T. thermophilus PRODH and P5CDH utilizing coexpression have also been studied and preliminary results reported. Finally, the structure determination of Bradyrhizobium japonicum PutA from pseudomerohedrally twinned crystal is reported.eng
dc.description.bibrefIncludes bibliographical referenceseng
dc.identifier.merlinb66672028eng
dc.identifier.oclc316866859eng
dc.identifier.urihttps://hdl.handle.net/10355/4760
dc.identifier.urihttps://doi.org/10.32469/10355/4760eng
dc.languageEnglisheng
dc.publisherUniversity of Missouri--Columbiaeng
dc.relation.ispartofcommunityUniversity of Missouri--Columbia. Graduate School. Theses and Dissertationseng
dc.rightsOpenAccess.eng
dc.rights.licenseThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 3.0 License.
dc.sourceSubmitted by University of Missouri--Columbia Graduate School.eng
dc.subject.lcshMetabolismeng
dc.subject.lcshProlineeng
dc.titleStructural and functional studies of proline catabolic enzymeseng
dc.typeThesiseng
thesis.degree.disciplineBiochemistry (Agriculture) (MU)eng
thesis.degree.grantorUniversity of Missouri--Columbiaeng
thesis.degree.levelDoctoraleng
thesis.degree.namePh. D.eng


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