Aspartate Aminotransferase - Bridging Carbohydrate and Energy Metabolism in Plasmodium Falciparum
Carsten Wrenger, Ingrid B. Muller, Ariel M. Silber, Rositsa Jordanova, Victor S. Lamzin and Matthew R. Groves
Affiliation: European Molecular Biology Laboratory - Hamburg Outstation c/o DESY, Building 25A, Notkestrasse 85, D-22670 Hamburg, Germany
In this mini-review we briefly examine and summarize evidence on the role of the plasmodial aspartate aminotransferase (AspAT) of the malarial parasite. Recent data have provided information on the products of the purine salvage pathway as well as the glycolytic and oxidative phosphorylation pathways, suggesting that the reaction catalyzed by AspAT is an essential step in all these biochemical processes. While the biological role of the oxidative phosphorylation cycle still remains to be demonstrated, the presence of a single protein that is functional in multiple pathways (i.e. amino acid/purine/pyrimidine biosynthesis and carbohydrate metabolism) provides a high potential for the development of novel strategies to combat the spread of multi-drug resistant malaria.
Keywords: Carbohydrate metabolism, energy metabolism, malarial parasite, aspartate aminotransferase, aspartate aminotransferase (AspAT), glycolytic, oxidative phosphorylation pathway, multi-drug resistant, sporozoites, asymptomatic, hypoglycemia, Plasmodium falciparum, tricarboxylic acid (TCA) cycle
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