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Membrane-bound thioesterase activity in mycoplasmas.

S Rottem, S L Trotter, M F Barile

    Journal of Bacteriology
    |February 1, 1977
    PubMed
    Summary

    Thioesterase activity is present in mycoplasmas, particularly in Acholeplasma species. This cell membrane enzyme

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    Area of Science:

    • Microbiology
    • Enzymology
    • Cell Biology

    Background:

    • Mycoplasmas, a group of bacteria, exhibit diverse metabolic capabilities.
    • Thioesterase activity has been observed in various mycoplasma species, but its characteristics and localization are not fully understood.

    Purpose of the Study:

    • To investigate the presence, localization, and substrate specificity of thioesterase activity in mycoplasmas.
    • To explore the potential regulatory role of this enzyme in fatty acid metabolism and its relationship with membrane lipid physical state.

    Main Methods:

    • Enzyme assays were performed on various mycoplasma species.
    • Thioesterase activity in Acholeplasma laidlawii was characterized regarding its localization within the cell membrane.
    • Substrate specificity was determined using different fatty acid thioesters.
    • Arrhenius plots were used to analyze the effect of temperature on enzyme activity in membranes with altered lipid composition.

    Main Results:

    • Thioesterase activity was detected in all tested mycoplasmas, with highest levels in Acholeplasma species.
    • The enzyme in Acholeplasma laidlawii is membrane-bound and resistant to extraction.
    • The enzyme shows broad specificity for long-chain fatty acid thioesters, preferring myristyl and palmityl derivatives.
    • Phase transition temperatures for membrane lipids were observed at 12 and 18 degrees C in A. laidlawii membranes enriched with elaidic or palmitic acids, respectively.

    Conclusions:

    • Thioesterase activity is a common feature in mycoplasmas, with significant variation among species.
    • The membrane-bound thioesterase in A. laidlawii may play a role in regulating fatty acid metabolism.
    • The enzyme's activity might be influenced by the physical state of the cell membrane lipids.

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