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Inactivation of urease by catechol: Kinetics and structure
Luca Mazzei1, Michele Cianci2, Francesco Musiani1
1Laboratory of Bioinorganic Chemistry, Department of Pharmacy and Biotechnology, University of Bologna, Italy.
Journal of Inorganic Biochemistry
|November 27, 2016
Summary
Catechol irreversibly inactivates urease (urea-hydrolyzing enzyme) from bacteria and plants via a radical mechanism. This finding offers potential for developing new urease inhibitors.
Area of Science:
- Biochemistry
- Enzymology
- Structural Biology
Background:
- Urease is a nickel-containing enzyme crucial for urea hydrolysis, implicated in pathogen virulence and reduced soil nitrogen fertilization.
- Efficient urease inhibitors are needed to address these issues.
Purpose of the Study:
- To characterize the molecular interaction between urease and catechol, a model polyphenol.
- To elucidate the mechanism of urease inhibition by catechol.
Main Methods:
- Enzyme inhibition assays using urease from Sporosarcina pasteurii (SPU) and Canavalia ensiformis (JBU).
- Molecular characterization of the enzyme-inhibitor interaction.
- X-ray crystallography of the SPU-catechol complex at 1.50Å resolution.
Main Results:
- Catechol irreversibly inactivates both SPU and JBU.
- The inactivation proceeds via a complex, radical-based, autocatalytic multistep mechanism.
- The crystal structure reveals detailed structural insights into the enzyme-catechol complex and inhibition mechanism.
Conclusions:
- Catechol is a potent irreversible inhibitor of urease from both microbial and plant sources.
- The study elucidates a novel radical-based mechanism for urease inhibition.
- Structural data provides a basis for designing targeted urease inhibitors.
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