Plasmodium glutathione reductase

Plasmodium glutathione reductase is a homodimeric flavoenzyme essential for the malaria parasite's antioxidant defense system. It catalyzes the reduction of oxidized glutathione disulfide (GSSG) to reduced glutathione (GSH) using NADPH, maintaining the intracellular redox balance necessary for parasite survival. While structurally similar to the human enzyme, the Plasmodium enzyme contains notable differences at ligand-binding sites, which are exploited for selective inhibitor design. Glutathione reductase is not essential for parasite asexual blood stage growth but becomes critical for the mosquito oocyst stage. It is a validated antimalarial drug target due to its indispensable role in the parasite's protection from oxidative stress and its structural divergence from the host enzyme.

Other names

Glutathione reductase (Plasmodium)GR (Plasmodium)Plasmodium falciparum glutathione reductase

Inhibition of glutathione reductase disrupts the parasite's redox balance, impairs antioxidant defense, and leads to oxidative stress and death of the malaria parasite.