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dc.contributor.advisorTanner, John J., 1961-eng
dc.contributor.authorFelts, Richard Levi, 1979-eng
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 23, 2009)eng
dc.descriptionVita.eng
dc.descriptionThesis (Ph.D.) University of Missouri-Columbia 2007.eng
dc.description.abstractAcid phosphatases are important, ubiquitous, and diverse group of enzymes that catalyze the transfer of phosphoryl from phosphomonoester to water forming inorganic phosphate and alcohol. These enzymes play critical roles in numerous processes and pathways including virulence. It has been suggested that the pathogenic bacteria Francisella tularensis utilizes an acid phosphatase to aid in the escape from the phagasome. As part of this research, the three dimensional X-ray crystal structures of three phosphatases from F. tularensis were determined. The three structures from F. tularensis were AcpA, HAP, and class C. Parallel to those structural studies homologous structures of class C acid phosphatases were determined from Haemophilus influenzae and Bacillus anthracis, those structures are also reported here. In all five unique acid phosphatase structures were determined in this research project that have led to a better understanding of the novelty of catalytic mechanisms, a clearer understanding of substrate binding, and a new foundation for structural investigation.eng
dc.description.bibrefIncludes bibliographical references.eng
dc.identifier.merlinb66668293eng
dc.identifier.oclc316805238eng
dc.identifier.urihttps://hdl.handle.net/10355/4857
dc.identifier.urihttps://doi.org/10.32469/10355/4857eng
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.subject.lcshAcid phosphataseeng
dc.subject.lcshFrancisella tularensiseng
dc.titleStructural studies of acid phosphatases from pathogenic bacteriaeng
dc.typeThesiseng
thesis.degree.disciplineChemistry (MU)eng
thesis.degree.grantorUniversity of Missouri--Columbiaeng
thesis.degree.levelDoctoraleng
thesis.degree.namePh. D.eng


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