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Pyruvate dehydrogenase activity in Streptococcus mutans.

J Carlsson, U Kujala, M B Edlund

    Infection and Immunity
    |September 1, 1985
    PubMed
    Summary
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    Pyruvate dehydrogenase activity was observed in Streptococcus mutans and Escherichia coli. This enzyme

    Area of Science:

    • Microbiology
    • Biochemistry

    Background:

    • Streptococcus mutans and Escherichia coli are key bacterial species.
    • Understanding metabolic pathways is crucial for microbiology and biochemistry.

    Purpose of the Study:

    • To investigate pyruvate dehydrogenase activity in S. mutans and E. coli.
    • To determine factors influencing this enzyme's activity.

    Main Methods:

    • Bacterial cultures of S. mutans and E. coli were grown under aerobic and anaerobic conditions.
    • Cell extracts were analyzed for pyruvate dehydrogenase activity.
    • Enzyme induction and inhibition were studied using specific compounds.

    Main Results:

    • Pyruvate dehydrogenase activity, dependent on thiamine pyrophosphate, coenzyme A, and NAD, was detected in both bacterial strains.

    Related Experiment Videos

  • Pyruvate induced enzyme activity, with higher levels observed in aerobically grown cells compared to anaerobically grown cells.
  • Acetyl phosphate strongly inhibited the enzyme, an effect partially reversed by inorganic phosphate.

    • Conclusions:

    • Pyruvate dehydrogenase is present and functional in both S. mutans and E. coli.
    • Aerobic conditions and pyruvate enhance enzyme activity.
    • Metabolic regulation by acetyl phosphate and inorganic phosphate affects pyruvate dehydrogenase function.