| Literature DB >> 18336344 |
M E Meza-Avina1, L Wei, M G Buhendwa, E Poduch, A M Bello, E F Pai, L P Kotra.
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.Entities:
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Year: 2008 PMID: 18336344 DOI: 10.2174/138955708783744065
Source DB: PubMed Journal: Mini Rev Med Chem ISSN: 1389-5575 Impact factor: 3.862