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[New metalloendopeptidase of Morganella morganii ZM]

N M Zamaliutdinova, L F Minnullina, M R Sharipova

    Bioorganicheskaia Khimiia
    |April 22, 2015
    PubMed

    Insights

    Proteolytic activity was discovered in Morganella morganii ZM, inhibited by o-phenanthroline. This enzyme specifically cleaves musculoskeletal actin, offering insights into bacterial protease functions.

    Area of Science:

    • Microbiology
    • Biochemistry
    • Enzymology

    Background:

    • Morganella morganii ZM possesses proteolytic enzymes.
    • Understanding bacterial proteases is crucial for various biological processes.
    • Metalloproteinases play significant roles in cellular functions.

    Purpose of the Study:

    • To investigate the proteolytic activity in Morganella morganii ZM.
    • To characterize the intracellular proteases responsible for actin cleavage.
    • To identify and purify metalloproteinases from M. morganii ZM.

    Main Methods:

    • Proteolytic activity assays were performed.
    • Zymography with gelatin was used to identify proteolytic proteins.
    • Hydrophobic chromatography was employed for protein purification.

    Main Results:

    • Proteolytic activity in M. morganii ZM was identified and inhibited by o-phenanthroline.
    • Intracellular proteases from M. morganii ZM were found to cleave musculoskeletal actin.
    • A 35 kDa metalloproteinase was purified from M. morganii ZM cell lysate.

    Conclusions:

    • M. morganii ZM harbors a metalloproteinase with actin-cleaving activity.
    • The identified protease is distinct from grimelysin in its substrate specificity.
    • Further research into this metalloproteinase could reveal novel biological functions.

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