Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.23.38 extracted from

  • Moura, P.A.; Dame, J.B.; Fidock, D.A.
    Role of Plasmodium falciparum digestive vacuole plasmepsins in the specificity and antimalarial mode of action of cysteine and aspartic protease inhibitors (2009), Antimicrob. Agents Chemother., 53, 4968-4978.
    View publication on PubMedView publication on EuropePMC

Inhibitors

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

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-

Synonyms

Synonyms Comment Organism
plasmepsin I
-
Plasmodium falciparum

General Information

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