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Optimized PCR-based Detection of Mycoplasma
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Optimized PCR-based Detection of Mycoplasma

Published on: June 20, 2011

Carboxypeptidase activity in human mycoplasmas

K Shibata, T Watanabe

    Journal of Bacteriology
    |November 1, 1986
    PubMed

    Insights

    Mycoplasma salivarium possesses an arginine-specific carboxypeptidase enzyme. This enzyme breaks down N-benzoylglycyl-L-arginine into citrulline, ammonia, and ATP, and is present in several related Mycoplasma species.

    Area of Science:

    • Microbiology
    • Enzymology

    Background:

    • Mycoplasma species are known inhabitants of mucosal surfaces.
    • Understanding their enzymatic activities is crucial for host-pathogen interactions.

    Purpose of the Study:

    • To characterize the enzymatic activity of Mycoplasma salivarium on N-benzoylglycyl-L-arginine.
    • To identify the enzyme responsible for this activity and its presence in other Mycoplasma species.

    Main Methods:

    • Incubation of N-benzoylglycyl-L-arginine with Mycoplasma salivarium.
    • Analysis of reaction products (citrulline, ammonia, ATP).
    • Enzyme inhibition assays using EDTA.

    Main Results:

    • Mycoplasma salivarium hydrolyzed N-benzoylglycyl-L-arginine.
    • The reaction yielded citrulline, ammonia, and ATP.
    • Enzyme activity was inhibited by EDTA, indicating a metalloenzyme.
    • Similar activity was detected in Mycoplasma orale, M. buccale, M. faucium, and M. hominis.

    Conclusions:

    • Mycoplasma salivarium possesses an arginine-specific carboxypeptidase.
    • This enzyme is likely a metalloenzyme due to EDTA inhibition.
    • The presence of this enzyme is conserved across several oral Mycoplasma species.

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