Affordable Access

deepdyve-link deepdyve-link
Publisher Website

The exceptional properties of Plasmodium deoxyguanylate pathways as a potential area for metabolic and drug discovery studies.

Authors
Type
Published Article
Journal
Nucleic acids symposium series (2004)
Publication Date
Issue
53
Pages
39–40
Identifiers
DOI: 10.1093/nass/nrp020
PMID: 19749249
Source
Medline
License
Unknown

Abstract

In Plasmodium falciparum, deoxyguanylate was found to be a substrate for several DNA metabolizing enzymes. Guanylate kinase utilizes dGMP with very low specificity, which is estimated to be the lowest among well-known prokaryotic and eukaryotic enzymes. Furthermore, thymidylate kinase, which is a pyrimidine specific enzyme, was found to phosphorylate dGMP with a surprisingly high specificity similar to that of the natural substrate. The above mentioned distinctions are specific for the Plasmodium protozoa and provide an interesting method for tracking dGMP metabolism during development and a starting point for drug development.

Statistics

Seen <100 times