Abstract
Orotidine 5-monophosphate decarboxylase (ODCase) is among the most proficient enzymes, and catalyzes the decarboxylation of OMP to UMP. An overview of ODCase and various proposals for its catalytic mechanism of decarboxylation are briefly presented here. A number of inhibitors of ODCase and new developments in the X-ray structures of ODCases from different species are discussed in the context of their therapeutic potential against cancer and infectious diseases. Latest discoveries in the inhibition of ODCase, for example using the novel C6 substitutions on the uridine, open new doors for drug discovery targeting parasitic diseases such as malaria.
Keywords: Orotidine 5'-monophosphate decarboxylase, de novo nucleotide synthesis, pyrimidine nucleotides, drug design
Mini-Reviews in Medicinal Chemistry
Title: Inhibition of Orotidine 5-Monophosphate Decarboxylase and Its Therapeutic Potential
Volume: 8 Issue: 3
Author(s): L. P. Kotra, M. E. Meza-Avina, L. Wei, M. G. Buhendwa, E. Poduch, A. M. Bello and E. F. Pai
Affiliation:
Keywords: Orotidine 5'-monophosphate decarboxylase, de novo nucleotide synthesis, pyrimidine nucleotides, drug design
Abstract: Orotidine 5-monophosphate decarboxylase (ODCase) is among the most proficient enzymes, and catalyzes the decarboxylation of OMP to UMP. An overview of ODCase and various proposals for its catalytic mechanism of decarboxylation are briefly presented here. A number of inhibitors of ODCase and new developments in the X-ray structures of ODCases from different species are discussed in the context of their therapeutic potential against cancer and infectious diseases. Latest discoveries in the inhibition of ODCase, for example using the novel C6 substitutions on the uridine, open new doors for drug discovery targeting parasitic diseases such as malaria.
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Cite this article as:
Kotra P. L., Meza-Avina E. M., Wei L., Buhendwa G. M., Poduch E., Bello M. A. and Pai F. E., Inhibition of Orotidine 5-Monophosphate Decarboxylase and Its Therapeutic Potential, Mini-Reviews in Medicinal Chemistry 2008; 8 (3) . https://dx.doi.org/10.2174/138955708783744065
DOI https://dx.doi.org/10.2174/138955708783744065 |
Print ISSN 1389-5575 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5607 |
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