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    Probing the antibiotic target MurA from Staphylococcus aureus and Bacillus subtilis

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    Biery_Jennifer_J_2007_6599344.pdf (384.9Kb)
    Issue Date
    2007-05-31
    Author
    Biery, Jennifer J.
    Publisher
    University of Kansas
    Type
    Thesis
    Degree Level
    M.S.
    Discipline
    Medicinal Chemistry
    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
    MurA (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.
    Description
    Thesis (M.S.)--University of Kansas, Medicinal Chemistry, 2007
    URI
    http://hdl.handle.net/1808/31959
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    Lawrence, KS 66045
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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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