Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Ro 40-4388 | aspartic protease peptidomimetic compound that potently inhibits plasmepsin I. Antimalarial activity is not exerted through inhibition of plasmepsins | Plasmodium falciparum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Plasmodium falciparum | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
plasmepsin I | - |
Plasmodium falciparum |
General Information | Comment | Organism |
---|---|---|
malfunction | multiple plasmepsin knockout mutants lacking plasmepsins I-III and I-IV, respectively show a significant increased parasite susceptibility to cyteine protease inhibitors. A ninefold increase in the potency of the calpain inhibitor N-acetyl-leucinyl-leucinyl-norleucinal (ALLN) against parasites lacking all four plasmepsins (I-IV) is observed. It is hypothesized that plasmepsins and some cysteine proteases play redundant or complementary roles in the digestive vacuole and that the absence of all plasmepsins (I-IV) renders these parasites highly susceptible to N-acetyl-leucinyl-leucinyl-norleucinal-mediated inhibition of falcipains | Plasmodium falciparum |