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Uridine phosphorylase in biomedical, structural, and functional aspects: A review

Uridine phosphorylase in biomedical, structural, and functional aspects: A review Abstract The activation of xenobiotics often causes malignant tumor cells to resist chemotherapeutic treatment. Uridine phosphorylase is the key enzyme of pyrimidine metabolism and catalyzes the reversible phosphorylation of uridine with the formation of uracil and ribose-1-phosphate. High-selectivity anticancer agents based on uridine phosphorylase inhibitors are promising for treating both oncological and infection diseases. New medicinal preparations can be predicted and rationally developed only on the basis of detailed biomedical, structural, and functional knowledge about the biomacromolecular target enzyme-drug complex. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Crystallography Reports Springer Journals

Uridine phosphorylase in biomedical, structural, and functional aspects: A review

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References (85)

Publisher
Springer Journals
Copyright
2011 Pleiades Publishing, Ltd.
ISSN
1063-7745
eISSN
1562-689X
DOI
10.1134/s1063774511040122
Publisher site
See Article on Publisher Site

Abstract

Abstract The activation of xenobiotics often causes malignant tumor cells to resist chemotherapeutic treatment. Uridine phosphorylase is the key enzyme of pyrimidine metabolism and catalyzes the reversible phosphorylation of uridine with the formation of uracil and ribose-1-phosphate. High-selectivity anticancer agents based on uridine phosphorylase inhibitors are promising for treating both oncological and infection diseases. New medicinal preparations can be predicted and rationally developed only on the basis of detailed biomedical, structural, and functional knowledge about the biomacromolecular target enzyme-drug complex.

Journal

Crystallography ReportsSpringer Journals

Published: Jul 1, 2011

Keywords: Crystallography and Scattering Methods

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