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  • Karl Schmitz, Assistant Professor

    Assistant Professor
    University of Delaware
    327 Wolf Hall
    Newark, DE 19716
    (302) 831-6100


    B.S. - Rensselaer Polytechnic Institute; Ph.D. - Perleman School of Medicine, University of Pennsylvania

    Clp protease assembly and disassembly

    The mycobacterial Clp proteases are large oligomeric complexes that comprise a hexameric unfoldase (ClpX or ClpC1) and a heteromeric barrel-shaped peptidase (ClpP1P2). Biochemical evidence suggests that protease assembly is dynamic, and that the active form exists in equilibrium with unassembled inactive species. We aim to characterize the assembly and disassembly pathways, the kinetics of activation and inactivation, and the mechanisms by which substrates stimulate activity.

    Substrate identification and selectivity

    ​Clp proteases selectively recognize protein substrates, which minimizes wasteful and deleterious off-target proteolysis. However, few bona fide substrates are known in mycobacteria, and the rules that govern substrate discrimination are not understood. Through targeted screening and capture-based methods, we aim to identify novel physiological substrates. We use cell-based and phage-based screening approaches to define the sequence-based rules by which these proteases select substrates. We also aim to crystallize protease components in complex with substrate polypeptides, to determine the specific interactions and motifs that guide substrate recognition. These studies will help us understand the role that Clp proteases play in mycobacterial biology, and will guide the development of novel in vivo reporter substrates.

    High-throughput screening and compound characterization

    ​A major motivation for studying Clp protease function is to improve our ability to develop compounds that disrupt their activity in M. tuberculosis. While we have a rich toolbox of reagents and assays useful for probing protease activity in vitro, few of these tools are well-suited to high-throughput screening applications. We are working to develop robust assay platforms with higher signal-to-noise, improved dynamic range, and the ability to multiplex reporters for unfolding, peptidase, and protease activities. We also collaborate with talented synthetic chemists to characterize and optimize compounds that target these essential mycobacterial enzymes.



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  • Chemistry and Biochemistry
  • 102 Brown Laboratory
  • University of Delaware
  • Newark, DE 19716, USA
  • Phone: 302-831-1247
  • Undergraduate Program Inquiries 302-831-2465