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Updated: Aug 27, 2025

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Measuring In Vitro ATPase Activity for Enzymatic Characterization
Published on: August 23, 2016
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Proton Pumping ATPases: Rotational Catalysis, Physiological Roles in Oral Pathogenic Bacteria, and Inhibitors
1Division of Biochemistry, School of Pharmacy, Iwate Medical University.
Biological & Pharmaceutical Bulletin
|October 2, 2022
Summary
Proton pumping ATPases (F- and A-ATPases) have essential roles beyond energy production in oral bacteria, impacting acid tolerance and nutrient import. Inhibiting these ATPases effectively reduces the growth and survival of oral pathogens.
Area of Science:
- Biochemistry
- Microbiology
- Molecular Biology
Background:
- Proton pumping ATPases (F-type and V/A-type) utilize rotational catalysis for energy conversion.
- While essential for ATP synthesis in mammals, their role in anaerobic bacteria was considered non-vital.
- Recent research indicates crucial non-energy-generating functions for these ATPases in oral pathogenic bacteria.
Purpose of the Study:
- To review the rotational catalysis mechanism of bacterial F- and A-ATPases.
- To discuss the specific physiological roles of these ATPases in oral bacteria.
- To evaluate the efficacy of ATPase inhibitors against oral pathogens.
Main Methods:
- Analysis of existing literature on rotational catalysis and ATPase function.
- Focus on studies investigating F- and A-ATPase roles in oral bacteria like Streptococcus mutans and Porphyromonas gingivalis.
- Review of data on the impact of phytopolyphenols and bedaquiline on bacterial growth.
Main Results:
- F-ATPase is critical for acid tolerance in Streptococcus mutans.
- A-ATPase facilitates nutrient import in Porphyromonas gingivalis.
- Inhibitors like phytopolyphenols and bedaquiline significantly impede the growth and survival of oral pathogenic bacteria.
Conclusions:
- Bacterial F- and A-ATPases possess unique physiological roles in oral pathogens beyond ATP synthesis.
- The rotational catalysis mechanism is conserved but adapted for specific functions.
- Proton pumping ATPases represent promising therapeutic targets for novel oral antimicrobial agents.
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