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The exceptional properties of Plasmodium deoxyguanylate pathways as a potential area for metabolic and drug discovery studies
Author(s) -
Mahmoud Kandeel,
Yoshiaki Kitamura,
Yukio Kitade
Publication year - 2009
Publication title -
nucleic acids symposium series
Language(s) - English
Resource type - Journals
eISSN - 1746-8272
pISSN - 0261-3166
DOI - 10.1093/nass/nrp020
Subject(s) - plasmodium falciparum , enzyme , kinase , biology , substrate specificity , biochemistry , dna , plasmodium (life cycle) , computational biology , chemistry , parasite hosting , malaria , computer science , world wide web , immunology
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.

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