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Carboxypeptidase activity in human mycoplasmas
Journal of Bacteriology
|November 1, 1986
Summary
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.