Plasmodium vivax lactate dehydrogenase (PvLDH)

Plasmodium vivax lactate dehydrogenase (PvLDH) is an essential enzyme that catalyzes the conversion of pyruvate to lactate in the glycolytic pathway and enables the parasite to sustain anaerobic energy metabolism during its erythrocytic life cycle[2][3]. PvLDH is structurally distinct from human LDH, allowing for selective inhibitor or antibody development[1][3]. It is a validated therapeutic target for antimalarial drug discovery due to its essential function and is widely used as a biomarker for the diagnosis and monitoring of P. vivax infections[2]. Crystal structures have shown that the active site and cofactor binding pocket of PvLDH are highly similar to those of P. falciparum LDH but distinct from human homologs, providing opportunities for species-specific inhibitor design[1][3]. PvLDH forms the antigenic basis of several malaria rapid diagnostic tests, enabling species-specific malaria detection and quantification of parasite biomass in blood[2].

Other names

Plasmodium vivax LDHPvLDHpLDH (may also refer to "Plasmodium lactate dehydrogenase" in general but often used for P. vivax in diagnostics)

Competitive inhibition of the NADH-binding or substrate-binding active site, Allosteric regulation or disruption of cofactor and substrate binding