dc.contributor.advisor | Tanner, John J., 1961- | eng |
dc.contributor.author | Felts, Richard Levi, 1979- | eng |
dc.date.issued | 2007 | eng |
dc.date.submitted | 2007 Spring | eng |
dc.description | The 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.description | Title from title screen of research.pdf file (viewed on March 23, 2009) | eng |
dc.description | Vita. | eng |
dc.description | Thesis (Ph.D.) University of Missouri-Columbia 2007. | eng |
dc.description.abstract | Acid 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.bibref | Includes bibliographical references. | eng |
dc.identifier.merlin | b66668293 | eng |
dc.identifier.oclc | 316805238 | eng |
dc.identifier.uri | https://hdl.handle.net/10355/4857 | |
dc.identifier.uri | https://doi.org/10.32469/10355/4857 | eng |
dc.language | English | eng |
dc.publisher | University of Missouri--Columbia | eng |
dc.relation.ispartofcommunity | University of Missouri--Columbia. Graduate School. Theses and Dissertations | eng |
dc.rights | OpenAccess. | eng |
dc.rights.license | This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 3.0 License. | |
dc.subject.lcsh | Acid phosphatase | eng |
dc.subject.lcsh | Francisella tularensis | eng |
dc.title | Structural studies of acid phosphatases from pathogenic bacteria | eng |
dc.type | Thesis | eng |
thesis.degree.discipline | Chemistry (MU) | eng |
thesis.degree.grantor | University of Missouri--Columbia | eng |
thesis.degree.level | Doctoral | eng |
thesis.degree.name | Ph. D. | eng |