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Literature summary 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)

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.23.38 additional information plasmepsin I is a valid antimalarial drug target on two counts. First, inhibition of the enzyme correlates with inhibition of parasite growth. Second, specificity of inhibition over human aspartic proteinases is possible Plasmodium falciparum
3.4.23.38 Ro40-4388
-
 Plasmodium falciparum
3.4.23.38 Ro40-5576
-
 Plasmodium falciparum
3.4.23.39 Ro40-4388
-
 Plasmodium falciparum
3.4.23.39 Ro40-5576
-
 Plasmodium falciparum

Organism

EC Number Organism UniProt Comment Textmining
3.4.23.38 Plasmodium falciparum
-
-
-
3.4.23.39 Plasmodium falciparum
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.23.39 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]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.23.38 0.000008
-
 Ro40-5576
-
 Plasmodium falciparum
3.4.23.38 0.000009
-
 Ro40-4388
-
 Plasmodium falciparum
3.4.23.39 0.00025
-
 Ro40-5576
-
 Plasmodium falciparum
3.4.23.39 0.0007
-
 Ro40-4388
-
 Plasmodium falciparum