Skip to content
2000
Volume 8, Issue 3
  • ISSN: 1389-5575
  • E-ISSN: 1875-5607

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.

Loading

Article metrics loading...

/content/journals/mrmc/10.2174/138955708783744065
2008-03-01
2025-09-07
Loading full text...

Full text loading...

/content/journals/mrmc/10.2174/138955708783744065
Loading
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error
Please enter a valid_number test