LDH (Plasmodium falciparum)

Q71T02

Malaria is one of the most widespread infectious diseases affecting some 500 million people with an enormous cost in human suffering and economic hardship. Effective treatment of the disease is increasingly compromised by rising resistance of malaria parasites to currently available anti-malarials. The parasites are homolactate fermenters and rely on glycolysis for energy generation since the parasites appear to lack a functional citric acid cycle. The NAD+ consumed during glycolysis is reduced to NADH by lactate which, in turn, is oxidized to pyruvate. This reaction is catalyzed by lactate dehydrogenase (LDH). It has been demonstrated that inhibitors of this enzyme have parasiticidal activity. Since LDH from the malaria parasite Plasmodium falciparum (PfLDH) has notable structural and kinetic differences from human LDHs, the enzyme appears to be an attractive target for novel anti-malarial therapeutics. The parasite, P. falciparum, is the most lethal of malarial plasmodia being responsible for the cerebral form of the disease; consequently it has been the major focus of initial biochemical and genomic investigation. On the other hand, the parasite P. vivax is of great importance as it is the most widespread and common of the malarial plasmodia and, therefore, is responsible for the greatest burden of disease.

35 kDa

AAG14292.1

> 85% by SDS-PAGE & Coomassie stain

lactate dehydrogenase