Exploiting unique structural and functional properties of malarial glycolytic enzymes for antimalarial drug development.

ABSTRACT: Metabolic enzymes have been known to carry out a variety of functions besides their normal housekeeping roles known as "moonlighting functions." These functionalities arise from structural changes induced by posttranslational modifications and/or binding of interacting proteins. Glycolysis is the sole source of energy generation for malaria parasite Plasmodium falciparum, hence a potential pathway for therapeutic intervention. Crystal structures of several P. falciparum glycolytic enzymes have been solved, revealing that they exhibit unique structural differences from the respective host enzymes, which could be exploited for their selective targeting. In addition, these enzymes carry out many parasite-specific functions, which could be of potential interest to control parasite development

SUBMITTER: Alam A 

PROVIDER: S-EPMC4280493 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature