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dc.contributor.advisorSchonbrunn, Ernst
dc.contributor.authorBiery, Jennifer J.
dc.date.accessioned2008-03-01T17:25:53Z
dc.date.available2008-03-01T17:25:53Z
dc.date.issued2007-12-18
dc.date.submitted2007
dc.identifier.otherhttp://dissertations.umi.com/ku:2302
dc.identifier.urihttp://hdl.handle.net/1808/1991
dc.description.abstractMurA (UDP-N-acetylglucosamine enolpyruvyl transferase) catalyzes the first committed step in the biosynthesis of cell wall peptidoglycan. Because this pathway is absent in mammals, MurA is an attractive target for the development of antimicrobial agents. While Escherichia coli and all other gram-negative bacteria possess only one copy of the MurA gene, analyses of the genomes of several gram-positive bacteria reveal the existence of two MurA genes, termed MurA1 and MurA2. The research presented here focuses on the cloning, expression, purification and kinetic characterization of the MurA enzymes from two gram-positive organisms: Staphylococcus aureus and Bacillus subtilis. Sequence analysis indicates that all genes are complete and that the enzymes contain the important catalytic residues previously identified in E. cloacae MurA. Kinetic characterization revealed that the enzymes from both organisms are active and are inhibited by fosfomycin.
dc.format.extent60 pages
dc.language.isoEN
dc.publisherUniversity of Kansas
dc.rightsThis item is protected by copyright and unless otherwise specified the copyright of this thesis/dissertation is held by the author.
dc.subjectMolecular biology
dc.subjectChemistry
dc.subjectBiochemistry
dc.subjectMura
dc.subjectB. subtilis
dc.subjectS. aureus
dc.subjectGram-positive
dc.titleProbing the Antibiotic Target MurA from S. aureus and B. subtilis
dc.typeThesis
dc.contributor.cmtememberScott, Emily E.
dc.contributor.cmtememberRichter, Mark
dc.thesis.degreeDisciplineMedicinal Chemistry
dc.thesis.degreeLevelM.S.
kusw.oastatusna
kusw.oapolicyThis item does not meet KU Open Access policy criteria.
kusw.bibid6599344
dc.rights.accessrightsopenAccess


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