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    TARGETING 5-ENOLPYRUVYLSHIKIMATE-3-PHOSPHATE SYNTHASE AND THE SHIKIMATE PATHWAY

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    Issue Date
    2008-08-21
    Author
    Funke, Todd Arnold
    Publisher
    University of Kansas
    Format
    243 pages
    Type
    Dissertation
    Degree Level
    PH.D.
    Discipline
    Molecular Biosciences
    Rights
    This item is protected by copyright and unless otherwise specified the copyright of this thesis/dissertation is held by the author.
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    Abstract
    Bacteria, plants, fungi, and apicomplexan parasites require the functionality of the shikimate pathway for biosynthesis of essential aromatic compounds. Animals lack the enzymes that constitute the shikimate pathway, making these attractive antimicrobial targets. Glyphosate (the active ingredient in Roundup herbicide) inhibits the shikimate pathway enzyme 5-enolpyruvyl-shikimate-3-phosphate synthase (EPSPS), but has limited antimicrobial activity. Several EPSPS point-substitutions can induce glyphosate tolerance, and some species possess EPSPS with intrinsic glyphosate insensitivity. To aid development of second-generation EPSPS inhibitors, I probed the inhibition of glyphosate-tolerant EPSPS. I examined the effects of mutations at Pro101 and Thr97 on the structure, function, and glyphosate sensitivity of E. coli EPSPS; I kinetically characterized the glyphosate-tolerant Staphylococcus aureus EPSPS and Agrobacterium sp. strain CP4 EPSPS and determined the three-dimensional structure of the CP4 enzyme; I studied the interaction of EPSPS with analogs of the substrate and the tetrahedral intermediate; and I conducted high throughput screening to identify novel EPSPS inhibitors.
    URI
    http://hdl.handle.net/1808/4185
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    • Dissertations [4454]
    • Molecular Biosciences Dissertations and Theses [270]

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    785-864-8983

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    Contact KU ScholarWorks
    785-864-8983
    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    785-864-8983

    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    Image Credits
     

     

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