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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Engineering
Engineering on EC 3.4.23.B19 - plasmepsin V
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C178A
the mutant shows reduced activity compared to the wild type enzyme
C178S
the mutant shows increased activity compared to the wild type enzyme
D108A
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mutation renders expressed protein catalytically inactive. Mutant localizes to the endoplasmic reticulum but the mutant has 3fold reduced signal by immunofluorescence and by western blot. Mutant enzyme-expressing parasites are frequently seen encased in erythrocyte ghosts, suggesting impaired host cell homeostasis. The levels of host erythrocyte histidine-rich protein II and another exported protein, RESA (ring-infected erythrocyte surface antigen), are diminished in the mutated PM V-expressing parasitized erythrocytes by 30-50%. Episomal expression of catalytically dead PM V has a dominant-negative effect on parasite growth and on protein export
D118N
the mutant shows reduced activity compared to the wild type enzyme
D118N/D365N
the mutant shows reduced activity compared to the wild type enzyme
D365N
the mutant shows reduced activity compared to the wild type enzyme
additional information
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identification of the region responsible for endoplasmic reticulum targeting: full-length PM V-GFP integrants and integrants with deletion of the C-terminus downstream of the membrane-spanning segment have no phenotype and retain endoplasmic reticulum targeting. Deletions involving the membrane anchor are lethal. Fusion of the transmembrane region but not other portions of PM V is sufficient to target a reporter to the endoplasmic reticulum