Information on EC 3.4.23.B19 - plasmepsin V

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The expected taxonomic range for this enzyme is: Plasmodium falciparum

EC NUMBER
COMMENTARY hide
3.4.23.B19
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
plasmepsin V
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cleavage of hemoglobin. In contrast to the food vacuole plasmepsins, detergent-solubilized PM V does not bind the aspartic protease inhibitor pepstatin.
show the reaction diagram
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-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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deletions involving the membrane anchor are lethal
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
DABCYL-LNKRLLHETQ-EDANS + H2O
?
show the reaction diagram
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fluorogenic peptide corresponding to the PEXEL motif for histidine-rich protein II is cleaved by PM V. Mutation of P1 Leu or P3 Arg abolishes cleavage
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-
?
DABCYL-RYVRILSETE-EDANS + H2O
?
show the reaction diagram
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fluorogenic peptide corresponding to the PEXEL motif for PfEMP2 is cleaved by PM V. Mutation of P1 Leu or P3 Arg abolishes cleavage
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-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
PM V pull-downs identified an ER-resident HSP70 and HSP101 as associated proteins
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-
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
nelfinavir
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pepstatin A
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saquinavir
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additional information
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in contrast to the food vacuole plasmepsins, detergent-solubilized PM V does not bind the aspartic protease inhibitor pepstatin
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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expressed over the course of asexual intraerythrocytic development
Manually annotated by BRENDA team
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the amount of PM V in the parasite is lowest in the ring stage and increases steadily through schizogony
Manually annotated by BRENDA team
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in trophozoites and schizonts, PM V is concentrated around the nucleus with lower levels dispersed in the surrounding cytoplasm
Manually annotated by BRENDA team
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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
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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integral membrane protein
Manually annotated by BRENDA team
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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