3.4.23.B19: plasmepsin V
This is an abbreviated version!
For detailed information about plasmepsin V, go to the full flat file.
Word Map on EC 3.4.23.B19
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3.4.23.B19
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plasmepsins
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plasmodium
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malaria
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falciparum
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erythrocyte
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pexel
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antimalarial
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vacuole
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aspartyl
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parasitophorous
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vivax
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translocon
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pepstatin
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asexual
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toxoplasma
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hydroxyethylamine
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peptidomimetics
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phosphatidylinositol-3-phosphate
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cytoadherence
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exportome
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picomolar
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intraerythrocytic
- 3.4.23.B19
-
plasmepsins
- plasmodium
- malaria
- falciparum
- erythrocyte
-
pexel
-
antimalarial
- vacuole
-
aspartyl
-
parasitophorous
- vivax
-
translocon
- pepstatin
-
asexual
- toxoplasma
-
hydroxyethylamine
-
peptidomimetics
- phosphatidylinositol-3-phosphate
-
cytoadherence
-
exportome
-
picomolar
-
intraerythrocytic
Reaction
cleavage of hemoglobin. In contrast to the food vacuole plasmepsins, detergent-solubilized PM V does not bind the aspartic protease inhibitor pepstatin. =
Synonyms
plasmepsin V, Plm V, PlmV, PM V, PMV, PMVm84, PMVp37
ECTree
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General Information on EC 3.4.23.B19 - plasmepsin V
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malfunction
metabolism
physiological function
malfunction
disruption of the enzyme gene leads to a developmental arrest in the subsequent erythrocytic cycle
malfunction
plasmepsin V inhibition blocks export of malaria proteins to human erythrocytes and inhibits parasite growth
malfunction
plasmepsin V inhibition blocks export of malaria proteins to human erythrocytes and inhibits parasite growth
metabolism
the enzyme cleaves malaria effector proteins in a distinct endoplasmic reticulum translocation interactome for export to the erythrocyte
metabolism
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the enzyme is responsible for the cleavage of Plasmodium export element-tagged proteins destined for export outside of the host red blood cell
metabolism
the enzyme is responsible for the cleavage of the Plasmodium export element (PEXEL) motif at the N-terminus of several hundreds of the exported proteins
physiological function
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PM V is the enzyme that processes PEXEL containing proteins to send them on their way for export into the host cell
physiological function
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plasmepsin V recognizes pentameric motif RxLxE/Q/D of exported proteins. Plasmepsin V cleavage reveals the export signal xE/Q/D at the N-terminus of cargo proteins. Plasmepsin V activity is essential and linked with other key export events
physiological function
the enzyme is essential for the survival, development and virulence of the parasite in the erythrocyte
physiological function
the enzyme processes proteins for export into the host erythrocyte and plays a crucial role in parasite virulence and survival
