Literature summary for 3.4.23.B19 extracted from

Klemba, M.; Goldberg, D.E.
Characterization of plasmepsin V, a membrane-bound aspartic protease homolog in the endoplasmic reticulum of Plasmodium falciparum. (2005), Mol. Biochem. Parasitol., 143, 183-191.

Search for more literature for 3.4.23.B19

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	in contrast to the food vacuole plasmepsins, detergent-solubilized PM V does not bind the aspartic protease inhibitor pepstatin	Plasmodium falciparum

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
endoplasmic reticulum	in intraerythrocytic parasites, PM V is located in the endoplasmic reticulum but not in ERD2-associated Golgi structures	Plasmodium falciparum	5783	-
membrane	integral membrane protein	Plasmodium falciparum	16020	-

Organism

Organism	UniProt	Comment	Textmining
Plasmodium falciparum	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
erythrocytic stage	expressed over the course of asexual intraerythrocytic development	Plasmodium falciparum	-
ring stage	the amount of PM V in the parasite is lowest in the ring stage and increases steadily through schizogony	Plasmodium falciparum	-
schizont	in trophozoites and schizonts, PM V is concentrated around the nucleus with lower levels dispersed in the surrounding cytoplasm	Plasmodium falciparum	-
trophozoite	the amount of PM V in the parasite is lowest in the ring stage and increases steadily through schizogony. In trophozoites and schizonts, PM V is concentrated around the nucleus with lower levels dispersed in the surrounding cytoplasm	Plasmodium falciparum	-

Synonyms

Synonyms	Comment	Organism
plasmepsin V	-	Plasmodium falciparum
PM V	-	Plasmodium falciparum

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Release 2023.1 (January 2023)