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Information on EC 3.4.23.B19 - plasmepsin V
for references in articles please use BRENDA:EC3.4.23.B19preliminary BRENDA-supplied EC number
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EC Tree
3.4.23.B19 plasmepsin VSpecify your search results
Word Map
- 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
The expected taxonomic range for this enzyme is: Plasmodium
Reaction Schemes
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, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PMV
PMVm84
PMV
-
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REACTION
REACTION DIAGRAM
COMMENTARY
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.
-
-
-
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DABCYL-LNKRLLHETQ-EDANS + H2O
?
-
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
-
-
?
Dabcyl-LNKRLLVETQE-Edans + H2O
?
about 150% activity compared to the HRPII peptide Dabcyl-LNKRLLHETQE-Edans
-
-
?
Dabcyl-RYVRELSETE-Edans + H2O
?
about 68% activity compared to the EMP2 peptide Dabcyl-RYVRILSETE-Edans
-
-
?
Dabcyl-RYVRELSETEE-Edans + H2O
?
about 10-25% activity compared to the EMP2 peptide Dabcyl-RYVRILSETEE-Edans
-
-
?
Dabcyl-RYVRILEETE-Edans + H2O
?
about 28% activity compared to the EMP2 peptide Dabcyl-RYVRILSETE-Edans
-
-
?
Dabcyl-RYVRILEETEE-Edans + H2O
?
about 7-30% activity compared to the EMP2 peptide Dabcyl-RYVRILSETEE-Edans
-
-
?
DABCYL-RYVRILSETE-EDANS + H2O
?
-
fluorogenic peptide corresponding to the PEXEL motif for PfEMP2 is cleaved by PM V. Mutation of P1 Leu or P3 Arg abolishes cleavage
-
-
?
Dabcyl-RYVRILVETE-Edans + H2O
?
about 28% activity compared to the EMP2 peptide Dabcyl-RYVRILSETE-Edans
-
-
?
Dabcyl-RYVRILVETEE-Edans + H2O
?
about 8-30% activity compared to the EMP2 peptide Dabcyl-RYVRILSETEE-Edans
-
-
?
Dabcyl-RYVRKLSETE-Edans + H2O
?
about 70% activity compared to the EMP2 peptide Dabcyl-RYVRILSETE-Edans
-
-
?
Dabcyl-RYVRKLSETEE-Edans + H2O
?
about 70% activity compared to the EMP2 peptide Dabcyl-RYVRILSETEE-Edans
-
-
?
EMP2 + H2O
Dabcyl-RYVRIL + SETE-Edans
i.e. Dabcyl-RYVRILSETE-Edans
-
-
?
erythrocyte membrane protein 2 + H2O
?
i.e. Dabcyl-RYVRILSETEE-Edans
-
-
?
histidine-rich protein II + H2O
?
i.e. Dabcyl-LNKRLLHETQE-Edans
-
-
?
Dabcyl-LNKRELHETQE-Edans + H2O
?
about 50% activity compared to the HRPII peptide Dabcyl-LNKRLLHETQE-Edans
-
-
?
Dabcyl-LNKRELHETQE-Edans + H2O
?
Plasmodium vivax Thai
about 50% activity compared to the HRPII peptide Dabcyl-LNKRLLHETQE-Edans
-
-
?
Dabcyl-LNKRKLHETQE-Edans + H2O
?
about 130% activity compared to the HRPII peptide Dabcyl-LNKRLLHETQE-Edans
-
-
?
Dabcyl-LNKRKLHETQE-Edans + H2O
?
Plasmodium vivax Thai
about 130% activity compared to the HRPII peptide Dabcyl-LNKRLLHETQE-Edans
-
-
?
Dabcyl-LNKRLLEETQE-Edans + H2O
?
about 50% activity compared to the HRPII peptide Dabcyl-LNKRLLHETQE-Edans
-
-
?
Dabcyl-LNKRLLEETQE-Edans + H2O
?
Plasmodium vivax Thai
about 50% activity compared to the HRPII peptide Dabcyl-LNKRLLHETQE-Edans
-
-
?
Dabcyl-LNKRLLSETQE-Edans + H2O
?
about 180% activity compared to the HRPII peptide Dabcyl-LNKRLLHETQE-Edans
-
-
?
Dabcyl-LNKRLLSETQE-Edans + H2O
?
Plasmodium vivax Thai
about 180% activity compared to the HRPII peptide Dabcyl-LNKRLLHETQE-Edans
-
-
?
EMP2 + H2O
?
i.e. Dabcyl-RYVRILSETE-Edans, most efficient substrate. Replacing Ser by Val or Glu of the PfEMP2 peptide P1' position markedly reduces the enzyme activity of the enzyme
-
-
?
HRPII + H2O
?
i.e. Dabcyl-LNKRLLHETQE-Edans. Replacing His by Val or Ser of the HRPII peptide P1' position increases the cleavage activity
-
-
?
additional information
?
-
-
PM V pull-downs identified an ER-resident HSP70 and HSP101 as associated proteins
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
no activity with DABCYL-KAVHYLEHNVKE-EDANS and Dabcyl-RYVAIASATEE-Edans
-
-
?
additional information
?
-
-
no activity with DABCYL-KAVHYLEHNVKE-EDANS and Dabcyl-RYVAIASATEE-Edans
-
-
?
additional information
?
-
no activity with DABCYL-KAVHYLEHNVKE-EDANS and Dabcyl-RYVAIASATEE-Edans
-
-
?
additional information
?
-
-
no activity with DABCYL-KAVHYLEHNVKE-EDANS and Dabcyl-RYVAIASATEE-Edans
-
-
?
additional information
?
-
Plasmodium vivax Thai
no activity with DABCYL-KAVHYLEHNVKE-EDANS and Dabcyl-RYVAIASATEE-Edans
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
erythrocyte membrane protein 2 + H2O
?
i.e. Dabcyl-RYVRILSETEE-Edans
-
-
?
histidine-rich protein II + H2O
?
i.e. Dabcyl-LNKRLLHETQE-Edans
-
-
?
additional information
?
-
-
PM V pull-downs identified an ER-resident HSP70 and HSP101 as associated proteins
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-(3-hydroxy-1,4-dioxo-1,4-dihydronaphthalen-2-yl)-2,2-dimethylpropyl heptanoate
58.6% residual activity at 0.05 mM
3-(3-hydroxy-1,4-dioxo-1,4-dihydronaphthalen-2-yl)-2,2-dimethylpropyl tridecanoate
49.5% residual activity at 0.05 mM
3-amino-N-[(benzyloxy)carbonyl]-L-phenylalanyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
-
4-amino-N-[(benzyloxy)carbonyl]-L-phenylalanyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
-
menisporopsin A
10-30% inhibition at 0.01 mM, 40-60% inhibition at 0.1 mM
N'-benzyl-2-(8-methyl-2,4-dioxo-1,3-diazaspiro[4.5]dec-3-yl)-N'-phenylacetohydrazide
ZINC36767691
N-(2-[[(2-fluorophenyl)methyl]amino]-2-oxoethyl)-2-iodobenzamide
ZINC07922110
N-[(benzyloxy)carbonyl]-3-carbamimidamido-L-phenylalanyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
-
N-[(benzyloxy)carbonyl]-4-carbamimidamido-L-phenylalanyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
-
N-[(benzyloxy)carbonyl]-O-carbamimidamido-L-homoseryl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
-
N2-[(benzyloxy)carbonyl]-L-arginyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
-
N2-[(benzyloxy)carbonyl]-N-carbamimidoyl-L-glutaminyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
-
N2-[(benzyloxy)carbonyl]-N5-(methylsulfonyl)-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
-
N2-[(benzyloxy)carbonyl]-N5-(N-cyanocarbamimidoyl)-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
-
N2-[(benzyloxy)carbonyl]-N5-(N-hydroxycarbamimidoyl)-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
-
N2-[(benzyloxy)carbonyl]-N5-(N-methoxycarbamimidoyl)-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
-
N2-[(benzyloxy)carbonyl]-N5-(N-methylcarbamimidoyl)-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
-
N2-[(benzyloxy)carbonyl]-N5-(N-nitrocarbamimidoyl)-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
-
N2-[(benzyloxy)carbonyl]-N5-(propan-2-yl)-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
-
N2-[(benzyloxy)carbonyl]-N5-carbamimidoyl-N5-methyl-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
-
N2-[(benzyloxy)carbonyl]-N5-carbamoyl-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
-
N2-[(benzyloxy)carbonyl]-N5-ethanimidoyl-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
-
N5-acetyl-N2-[(benzyloxy)carbonyl]-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
-
tert-butyl (3-[[(2-methyl-1H-indol-3-yl)carbonyl]amino]propyl)(pyridin-3-ylmethyl)carbamate
ZINC72012008
nelfinavir
the truncated enzyme PMVm84 exhibits about 53% residual activity at 0.1 mM
phenylmethylsulfonyl fluoride
the truncated enzyme PMVm84 exhibits about 70% residual activity at 0.1 mM
phenylmethylsulfonyl fluoride
about 20% inhibition at 0.01 mM, 50-70% inhibition at 0.1 mM
additional information
-
in contrast to the food vacuole plasmepsins, detergent-solubilized PM V does not bind the aspartic protease inhibitor pepstatin
-
additional information
not influenced by Ca2+; pepstatin A cannot inhibit refolded enzyme activity
-
additional information
-
not influenced by Ca2+; pepstatin A cannot inhibit refolded enzyme activity
-
additional information
the truncated enzyme PMVm84 is not inhibited by pepstatin A
-
additional information
-
the truncated enzyme PMVm84 is not inhibited by pepstatin A
-
additional information
not inhibited by pepstatin A and nelfinavir
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Malaria
Correction: Picomolar Inhibition of Plasmepsin V, an Essential Malaria Protease, Achieved Exploiting the Prime Region.
Malaria
Enhanced antimalarial activity of plasmepsin V inhibitors by modification of the P2 position of PEXEL peptidomimetics.
Malaria
Flap flexibility amongst plasmepsins I, II, III, IV, and V: Sequence, structural, and molecular dynamics analyses.
Malaria
In silico validation of novel inhibitors of malarial aspartyl protease, plasmepsin V and antimalarial efficacy prediction.
Malaria
Inhibition of Plasmepsin V activity demonstrates its essential role in protein export, PfEMP1 display, and survival of malaria parasites.
Malaria
Picomolar Inhibition of Plasmepsin V, an Essential Malaria Protease, Achieved Exploiting the Prime Region.
Malaria
Plasmepsin V cleaves malaria effector proteins in a distinct endoplasmic reticulum translocation interactome for export to the erythrocyte.
Malaria
Structural basis for plasmepsin V inhibition that blocks export of malaria proteins to human erythrocytes.
Malaria
The C-terminal portion of the cleaved HT motif is necessary and sufficient to mediate export of proteins from the malaria parasite into its host cell.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02225
3-(3-hydroxy-1,4-dioxo-1,4-dihydronaphthalen-2-yl)-2,2-dimethylpropyl heptanoate
Plasmodium falciparum
at pH 6.5 and 25°C
0.06894
3-(3-hydroxy-1,4-dioxo-1,4-dihydronaphthalen-2-yl)-2,2-dimethylpropyl tridecanoate
Plasmodium falciparum
at pH 6.5 and 25°C
0.05
3-amino-N-[(benzyloxy)carbonyl]-L-phenylalanyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
Plasmodium falciparum
IC50 above 0.05 mM, at pH 6.4 and 37°C
0.05
4-amino-N-[(benzyloxy)carbonyl]-L-phenylalanyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
Plasmodium falciparum
IC50 above 0.05 mM, at pH 6.4 and 37°C
0.0856
N'-benzyl-2-(8-methyl-2,4-dioxo-1,3-diazaspiro[4.5]dec-3-yl)-N'-phenylacetohydrazide
Plasmodium falciparum
pH and temperature not specified in the publication
0.05
N-[(benzyloxy)carbonyl]-3-carbamimidamido-L-phenylalanyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
Plasmodium falciparum
IC50 above 0.05 mM, at pH 6.4 and 37°C
0.05
N-[(benzyloxy)carbonyl]-4-carbamimidamido-L-phenylalanyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
Plasmodium falciparum
IC50 above 0.05 mM, at pH 6.4 and 37°C
0.00274
N-[(benzyloxy)carbonyl]-O-carbamimidamido-L-homoseryl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
Plasmodium falciparum
at pH 6.4 and 37°C
0.000128
N2-[(benzyloxy)carbonyl]-L-arginyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
Plasmodium falciparum
at pH 6.4 and 37°C
0.0416
N2-[(benzyloxy)carbonyl]-N-carbamimidoyl-L-glutaminyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
Plasmodium falciparum
at pH 6.4 and 37°C
0.05
N2-[(benzyloxy)carbonyl]-N5-(methylsulfonyl)-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
Plasmodium falciparum
IC50 above 0.05 mM, at pH 6.4 and 37°C
0.05
N2-[(benzyloxy)carbonyl]-N5-(N-cyanocarbamimidoyl)-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
Plasmodium falciparum
IC50 above 0.05 mM, at pH 6.4 and 37°C
0.00388
N2-[(benzyloxy)carbonyl]-N5-(N-hydroxycarbamimidoyl)-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
Plasmodium falciparum
at pH 6.4 and 37°C
0.18
N2-[(benzyloxy)carbonyl]-N5-(N-methoxycarbamimidoyl)-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
Plasmodium falciparum
at pH 6.4 and 37°C
0.0377
N2-[(benzyloxy)carbonyl]-N5-(N-methylcarbamimidoyl)-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
Plasmodium falciparum
at pH 6.4 and 37°C
0.05
N2-[(benzyloxy)carbonyl]-N5-(N-nitrocarbamimidoyl)-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
Plasmodium falciparum
IC50 above 0.05 mM, at pH 6.4 and 37°C
0.05
N2-[(benzyloxy)carbonyl]-N5-(propan-2-yl)-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
Plasmodium falciparum
IC50 above 0.05 mM, at pH 6.4 and 37°C
0.05
N2-[(benzyloxy)carbonyl]-N5-carbamimidoyl-N5-methyl-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
Plasmodium falciparum
IC50 above 0.05 mM, at pH 6.4 and 37°C
0.05
N2-[(benzyloxy)carbonyl]-N5-carbamoyl-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
Plasmodium falciparum
at pH 6.4 and 37°C
0.0403
N2-[(benzyloxy)carbonyl]-N5-ethanimidoyl-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
Plasmodium falciparum
at pH 6.4 and 37°C
0.05
N5-acetyl-N2-[(benzyloxy)carbonyl]-L-ornithyl-N-[(3S,4S)-3-hydroxy-6-methyl-1-oxo-1-[(2-phenylethyl)amino]heptan-4-yl]-L-valinamide
Plasmodium falciparum
IC50 above 0.05 mM, at pH 6.4 and 37°C
0.0487
tert-butyl (3-[[(2-methyl-1H-indol-3-yl)carbonyl]amino]propyl)(pyridin-3-ylmethyl)carbamate
Plasmodium falciparum
pH and temperature not specified in the publication
0.00001
WEHI-842
Plasmodium falciparum
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0009
mutant enzyme D118N/D365N, with HRPII as substrate, at pH 6.5 and 25°C
0.01
mutant enzyme D118N/D365N, with EMP2 as substrate, at pH 6.5 and 25°C
0.022
mutant enzyme D365N, with HRPII as substrate, at pH 6.5 and 25°C
0.027
mutant enzyme D365N, with EMP2 as substrate, at pH 6.5 and 25°C
0.041
mutant enzyme D118N, with HRPII as substrate, at pH 6.5 and 25°C
0.05
mutant enzyme D118N, with EMP2 as substrate, at pH 6.5 and 25°C
0.055
mutant enzyme C178A, with HRPII as substrate, at pH 6.5 and 25°C
0.083
wild type enzyme, with HRPII as substrate, at pH 6.5 and 25°C
0.088
mutant enzyme C178A, with EMP2 as substrate, at pH 6.5 and 25°C
0.09
0.114
mutant enzyme C178S, with EMP2 as substrate, at pH 6.5 and 25°C
0.09
mutant enzyme C178S, with HRPII as substrate, at pH 6.5 and 25°C
0.09
wild type enzyme, with EMP2 as substrate, at pH 6.5 and 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolate 3D7
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
expressed over the course of asexual intraerythrocytic development
brenda
-
the amount of PM V in the parasite is lowest in the ring stage and increases steadily through schizogony
brenda
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in trophozoites and schizonts, PM V is concentrated around the nucleus with lower levels dispersed in the surrounding cytoplasm
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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
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme faces the endoplasmic reticulum lumen
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-
in intraerythrocytic parasites, PM V is located in the endoplasmic reticulum but not in ERD2-associated Golgi structures
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protein does not contain a classical endoplasmic reticulum retention signal. Transmembrane sequence is important for endoplasmic reticulum localization
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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
-
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
-
PM V is the enzyme that processes PEXEL containing proteins to send them on their way for export into the host cell
physiological function
-
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
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
-
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Hitrap Q column chromatography
HiTrap Q column chromatography and HisTrap column chromatography
Superdex 75 gel filtration
HisTrap column chromatography and Hitrap Q column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as thioredoxin fusion proteins in Escherichia coli BL21 (DE3) cells
expressed as thioredoxin fusion proteins in Escherichia coli L21(DE3) cells
expressed in Escherichia coli BL21 (DE3) cells
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
using a 10-volume rapid dilution into 20 mM Tris-HCl pH 8, 0.15 M NaCl, 1 mM GSH, 0.1 mM GSSG, and 10% (v/v) glycerol with gentle stirring at 25°C for 24 h
using a 10-volume rapid dilution into 20 mM Tris-HCl pH 8.0, 1 mM reduced glutathione, 0.1 mM oxidized glutathione, 0.15 M NaCl, and 10% (v/v) glycerol with stirring at 25°C for 24 h
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Klemba, M.; Goldberg, D.E.
Characterization of plasmepsin V, a membrane-bound aspartic protease homolog in the endoplasmic reticulum of Plasmodium falciparum.
Mol. Biochem. Parasitol.
143
183-191
2005
Plasmodium falciparum
brenda
Russo, I.; Babbitt, S.; Muralidharan, V.; Butler, T.; Oksman, A.; Goldberg, D.E.
Plasmepsin V licenses Plasmodium proteins for export into the host erythrocyte
Nature
463
632-636
2010
Plasmodium falciparum
brenda
Boddey, J.A.; Hodder, A.N.; Guenther, S.; Gilson, P.R.; Patsiouras, H.; Kapp, E.A.; Pearce, J.A.; de Koning-Ward, T.F.; Simpson, R.J.; Crabb, B.S.; Cowman, A.F.
An aspartyl protease directs malaria effector proteins to the host cell
Nature
463
627-631
2010
Plasmodium falciparum
brenda
Sittikul, P.; Songtawee, N.; Kongkathip, N.; Boonyalai, N.
In vitro and in silico studies of naphthoquinones and peptidomimetics toward Plasmodium falciparum plasmepsin V
Biochimie
152
159-173
2018
Plasmodium falciparum (Q8I6Z5), Plasmodium falciparum
brenda
Gazdik, M.; Jarman, K.E.; ONeill, M.T.; Hodder, A.N.; Lowes, K.N.; Jousset Sabroux, H.; Cowman, A.F.; Boddey, J.A.; Sleebs, B.E.
Exploration of the P3 region of PEXEL peptidomimetics leads to a potent inhibitor of the Plasmodium protease, plasmepsin V
Bioorg. Med. Chem.
24
1993-2010
2016
Plasmodium falciparum (Q8I6Z5)
brenda
Meissner, K.A.; Kronenberger, T.; Maltarollo, V.G.; Trossini, G.H.G.; Wrenger, C.
Targeting the Plasmodium falciparum plasmepsin V by ligand-based virtual screening
Chem. Biol. Drug Des.
93
300-312
2019
Plasmodium falciparum (Q8I6Z5), Plasmodium falciparum
brenda
Boonyalai, N.; Sittikul, P.; Yuvaniyama, J.
Plasmodium falciparum plasmepsin V (PfPMV) Insights into recombinant expression, substrate specificity and active site structure
Mol. Biochem. Parasitol.
201
5-15
2015
Plasmodium falciparum (Q8I6Z5), Plasmodium falciparum
brenda
Sappakhaw, K.; Takasila, R.; Sittikul, P.; Wattana-Amorn, P.; Assavalapsakul, W.; Boonyalai, N.
Biochemical characterization of plasmepsin V from Plasmodium vivax Thailand isolates Substrate specificity and enzyme inhibition
Mol. Biochem. Parasitol.
204
51-63
2015
Plasmodium vivax (A0A0H4FQ60), Plasmodium vivax, Plasmodium vivax Thai (A0A0H4FQ60)
brenda
Loymunkong, C.; Sittikul, P.; Songtawee, N.; Wongpanya, R.; Boonyalai, N.
Yield improvement and enzymatic dissection of Plasmodium falciparum plasmepsin V
Mol. Biochem. Parasitol.
231
111188
2019
Plasmodium falciparum (Q8I6Z5), Plasmodium falciparum
brenda
L, M.; Soliman, M.E.
The binding landscape of plasmepsin V and the implications for flap dynamics
Mol. Biosyst.
12
1457-1467
2016
Plasmodium vivax
brenda
Marapana, D.S.; Dagley, L.F.; Sandow, J.J.; Nebl, T.; Triglia, T.; Pasternak, M.; Dickerman, B.K.; Crabb, B.S.; Gilson, P.R.; Webb, A.I.; Boddey, J.A.; Cowman, A.F.
Plasmepsin V cleaves malaria effector proteins in a distinct endoplasmic reticulum translocation interactome for export to the erythrocyte
Nat. Microbiol.
3
1010-1022
2018
Plasmodium falciparum (Q8I6Z5), Plasmodium falciparum
brenda
Hodder, A.N.; Sleebs, B.E.; Czabotar, P.E.; Gazdik, M.; Xu, Y.; ONeill, M.T.; Lopaticki, S.; Nebl, T.; Triglia, T.; Smith, B.J.; Lowes, K.; Boddey, J.A.; Cowman, A.F.
Structural basis for plasmepsin V inhibition that blocks export of malaria proteins to human erythrocytes
Nat. Struct. Mol. Biol.
22
590-596
2015
Plasmodium vivax (Q6PRR9), Plasmodium vivax, Plasmodium falciparum (Q8I6Z5), Plasmodium falciparum
brenda
Tarr, S.J.; Osborne, A.R.
Experimental determination of the membrane topology of the Plasmodium protease plasmepsin V
PLoS ONE
10
e0121786
2015
Plasmodium falciparum (Q8I6Z5), Plasmodium falciparum
brenda
Boonyalai, N.; Collins, C.R.; Hackett, F.; Withers-Martinez, C.; Blackman, M.J.
Essentiality of Plasmodium falciparum plasmepsin V
PLoS ONE
13
e0207621
2018
Plasmodium falciparum (Q8I6Z5), Plasmodium falciparum
brenda
McGillewie, L.; Soliman, M.E.
Flap flexibility amongst plasmepsins I, II, III, IV, and V Sequence, structural, and molecular dynamics analyses
Proteins
83
1693-1705
2015
Plasmodium falciparum (Q8I6Z5), Plasmodium falciparum
brenda
Bedi, R.K.; Patel, C.; Mishra, V.; Xiao, H.; Yada, R.Y.; Bhaumik, P.
Understanding the structural basis of substrate recognition by Plasmodium falciparum plasmepsin V to aid in the design of potent inhibitors
Sci. Rep.
6
31420
2016
Plasmodium falciparum (Q8I6Z5), Plasmodium falciparum
brenda
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