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Prolipoprotein modification and processing enzymes in Escherichia coli.

M Tokunaga, J M Loranger, H C Wu

    The Journal of Biological Chemistry
    |March 25, 1984
    PubMed
    Summary

    Prolipoprotein signal peptidase, an enzyme in Escherichia coli, was characterized in vitro. Globomycin effectively inhibited this enzyme, crucial for processing prolipoprotein.

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    Area of Science:

    • Microbiology
    • Enzymology
    • Molecular Biology

    Background:

    • Prolipoprotein signal peptidase is a key enzyme in bacterial lipoprotein processing.
    • Its precise catalytic mechanisms and optimal conditions require further elucidation.

    Purpose of the Study:

    • To characterize the in vitro activity of prolipoprotein signal peptidase.
    • To investigate the enzyme's localization, substrate specificity, and inhibition by globomycin.
    • To analyze the activity of phosphatidylglycerol:prolipoprotein glyceryl transferase.

    Main Methods:

    • In vitro enzymatic assays using purified prolipoprotein as substrate.
    • Enzyme localization studies within the Escherichia coli cell envelope.
    • Inhibition assays with globomycin.
    • Measurement of glyceryl transferase activity using radiolabeled cell envelopes.

    Main Results:

    • Prolipoprotein signal peptidase activity was characterized in vitro, requiring nonionic detergents but not phospholipids.
    • The enzyme is localized in the inner cytoplasmic membrane of Escherichia coli.
    • Globomycin demonstrated potent inhibition with a half-maximal inhibiting concentration of 0.76 nM.
    • Optimal activity for prolipoprotein signal peptidase was observed at pH 7.9 and 37-45°C.
    • Phosphatidylglycerol:prolipoprotein glyceryl transferase activity was confirmed, with optimal conditions at pH 7.8 and 37°C.

    Conclusions:

    • Prolipoprotein signal peptidase is an essential, detergent-dependent enzyme in the inner cytoplasmic membrane of E. coli.
    • Globomycin is a highly effective inhibitor of this enzyme.
    • Characterization of glyceryl transferase provides further insight into lipoprotein modification.

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