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Structural and functional studies on urease from pigeon pea (Cajanus cajan)
Anuradha Balasubramanian1, Vishnuprabu Durairajpandian, Sagadevan Elumalai
1Centre of Advanced Study in Crystallography and Biophysics University of Madras, Guindy Campus, Chennai 600025, India.
International Journal of Biological Macromolecules
|April 30, 2013
Summary
Pigeon pea urease (PPU) crystal structure reveals insights into its antifungal activity. This plant urease also exhibits insecticidal and cellulase properties, independent of urea breakdown.
Area of Science:
- Biochemistry
- Structural Biology
- Enzymology
Background:
- Urease enzymes catalyze urea hydrolysis, producing ammonia and carbon dioxide.
- Plant and bacterial ureases share structural similarities but differ in insecticidal activity.
- Both plant and bacterial ureases possess antifungal properties, independent of ureolytic function.
Purpose of the Study:
- To determine the crystal structure of pigeon pea urease (PPU).
- To investigate the stability, insecticidal, and antifungal activities of PPU.
- To elucidate the mechanism behind the antifungal activity of urease.
Main Methods:
- X-ray crystallography to obtain the PPU crystal structure.
- Biochemical assays to assess PPU's stability, insecticidal, and antifungal activities.
- Molecular docking studies with cellopentaose to propose an antifungal mechanism.
Main Results:
- The crystal structure of pigeon pea urease (PPU) was determined.
- PPU demonstrated insecticidal and antifungal activities, along with cellulase activity.
- Structural analysis and docking suggest a potential mechanism for urease's antifungal action.
Conclusions:
- Pigeon pea urease possesses unique biological activities beyond ureolysis.
- The study provides structural insights into the antifungal mechanism of urease.
- Further research is warranted to fully understand the insecticidal and fungicidal properties of plant ureases.
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