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Updated: May 22, 2026
09:11
Screening for Thermotoga maritima Membrane-Bound Pyrophosphatase Inhibitors
Published on: November 23, 2019
Discovery of Two Thermophilic Inorganic Pyrophosphatases With Broad Temperature Adaptability
Fangli Wei1, Hua Dong1, Shuiqin Jiang1
1Research Center for Systems Biosynthesis, National Key Laboratory of Lead Druggability Research, China State Institute of Pharmaceutical Industry, Shanghai, China.
Chembiochem : a European Journal of Chemical Biology
|May 21, 2026
Summary
Two novel inorganic pyrophosphatases (PPases) from thermophilic organisms exhibit high stability and broad temperature adaptability. These enzymes efficiently hydrolyze pyrophosphate, showing potential for industrial and biotechnological applications.
Area of Science:
- Biochemistry
- Enzymology
- Molecular Biology
Background:
- Inorganic pyrophosphatases (PPases) are crucial enzymes that prevent cellular inorganic pyrophosphate (PPi) accumulation through hydrolysis.
- Pathological PPi buildup can disrupt cellular processes, necessitating effective PPi-degrading enzymes.
Purpose of the Study:
- To clone, express, and biochemically characterize two novel thermostable soluble inorganic pyrophosphatases (PPases) from Thermoleophilia bacterium (PPaseTba) and Thermoprotei archaeon (PPaseTar).
- To evaluate the enzymatic properties, including catalytic activity, thermostability, and pH tolerance, of the novel PPases.
Main Methods:
- Gene cloning and expression of PPaseTba and PPaseTar in a suitable host system.
- Biochemical assays to determine enzyme kinetics, optimal temperature, pH, and stability profiles.
- Analysis of enzyme activity across a range of temperatures, including moderate and high conditions.
Main Results:
- Both PPaseTba and PPaseTar demonstrated robust catalytic activity towards inorganic pyrophosphate (PPi).
- The enzymes exhibited exceptional thermostability and pH tolerance, with optimal activity at 85°C and pH 8.5.
- Remarkably, they retained 60-70% of maximal activity at 25°C, indicating broad temperature adaptability.
Conclusions:
- PPaseTba and PPaseTar possess unique properties of high thermostability and broad temperature adaptability, alongside efficient PPi hydrolysis.
- These characteristics enable the enzymes to overcome thermodynamic inhibition in biosynthetic systems under varying temperatures.
- The novel PPases hold significant potential for applications in industrial biocatalysis, molecular diagnostics, and RNA-based biotechnology, including biomedical research and biomanufacturing.
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