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Uridine phosphorylase from Schistosoma mansoni
M H el Kouni1, F N Naguib, J G Niedzwicki
1Division of Biology and Medicine, Brown University, Providence, Rhode Island 02912.
The Journal of Biological Chemistry
|May 5, 1988
Summary
Researchers identified and purified uridine phosphorylase from Schistosoma mansoni. This enzyme is crucial for pyrimidine nucleoside breakdown and shows potential as a target for new antiparasitic drugs.
Area of Science:
- Biochemistry
- Parasitology
- Drug Discovery
Background:
- Uridine phosphorylase is the sole detected pyrimidine nucleoside cleaving enzyme in Schistosoma mansoni.
- This enzyme is distinct from the parasite's purine nucleoside phosphorylases.
Purpose of the Study:
- To purify and characterize uridine phosphorylase from Schistosoma mansoni.
- To investigate its substrate specificity, kinetic properties, and potential as a drug target.
Main Methods:
- Enzyme purification using Sephadex G-100 chromatography.
- Kinetic analysis (Km, KPi, Vmax) with various substrates.
- Inhibitor screening using 5-(Benzyloxybenzyloxybenzyl)acyclouridine.
Main Results:
- Uridine phosphorylase was purified 170-fold with a molecular weight of 56,000.
- The enzyme prefers uridine but also processes deoxyuridine and deoxythymidine.
- A potent and specific inhibitor, 5-(Benzyloxybenzyloxybenzyl)acyclouridine, was identified.
Conclusions:
- Schistosoma mansoni uridine phosphorylase possesses unique structural features compared to mammalian enzymes.
- These differences enable the design of specific inhibitors targeting nucleic acid synthesis in the parasite.