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Literature summary for 3.4.23.39 extracted from

  • Moon, R.P.; Bur, D.; Loetscher, H.; D'Arcy, A.; Tyas, L.; Oefner, C.; Grueninger-Leitch, F.; Mona, D.; Rupp, K.; Dorn, A.; Matile, H.; Certa, U.; Berry, C.; Kay, J.; Ridley, R.G.
    Studies on plasmepsins I and II from the malarial parasite Plasmodium falciparum and their exploitation as drug targets (1998), Adv. Exp. Med. Biol., 436, 397-406.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
plasmepsin II in complex with pepstatin A Plasmodium falciparum

Inhibitors

Inhibitors Comment Organism Structure
Ro40-4388
-
Plasmodium falciparum
Ro40-5576
-
Plasmodium falciparum

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification recombinant proplasmepsin II autoactivates at acidic pH, but the location of the cleavage site varies dependening on the conditions used Plasmodium falciparum

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00025
-
Ro40-5576
-
Plasmodium falciparum
0.0007
-
Ro40-4388
-
Plasmodium falciparum