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Nucleic Acids Symposium Series 2009 53(1):39-40; doi:10.1093/nass/nrp020
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© 2009 Oxford University Press

This article appears in the following Nucleic Acid Symposium Series issue: The 6th International Symposium on Nucleic Acids Chemistry (36th Symposium on Nucleic Acids Chemistry) [View the issue table of contents]

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

Mahmoud Kandeel1,2, Yoshiaki Kitamura1 and Yukio Kitade1,2,3,4,*

1Department of Biomolecular Science, Faculty of Engineering, 2Center for Advanced Drug Research and 3Center for Emerging Infectious Diseases and 4United Graduate School of Drug Discovery and Medical Information Sciences, Gifu University, 1-1 Yanagido, Gifu 501-1193, Japan

*Corresponding author. E-mail: ykkitade{at}gifu-u.ac.jp

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.


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