3.4.23.B14: plasmepsin IV
This is an abbreviated version!
For detailed information about plasmepsin IV, go to the full flat file.
Word Map on EC 3.4.23.B14
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3.4.23.B14
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plasmepsins
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plasmodium
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falciparum
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malaria
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vacuole
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hemoglobin
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antimalarial
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cathepsin
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vivax
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ovale
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intraerythrocytic
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medicine
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peptidomimetic
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berghei
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hydroxyethylamine
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allophenylnorstatine
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histo-aspartic
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proplasmepsins
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analysis
- 3.4.23.B14
-
plasmepsins
- plasmodium
- falciparum
- malaria
- vacuole
- hemoglobin
-
antimalarial
- cathepsin
- vivax
- ovale
-
intraerythrocytic
- medicine
-
peptidomimetic
- berghei
-
hydroxyethylamine
-
allophenylnorstatine
-
histo-aspartic
-
proplasmepsins
- analysis
Reaction
cleavage of hemoglobin. In the S3 and S2 subsites, the plasmepsin 4 orthologs all prefer hydrophobic amino acid residues, Phe or Ile, but reject charged residues such as Lys or Asp. In S2' and S3' subsites these plasmepsins tolerate both hydrophobic and hydrophilic residues =
Synonyms
A01.059, PfPM4, PgPM4, plasmepsin 4, Plm IV, PM IV, PM-IV, PM4, PMIV, PmPM4, PoPM4, pPM IV, proplasmepsin IV, PSM4, PvPM4
ECTree
3.4.23.B14 plasmepsin IVAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.23.B14 - plasmepsin IV
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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
denatured human hemoglobin + H2O
?
preferred over native human hemoglobin. PvPM4 acts synergistically with cysteine proteases vivapain-2 and vivapain-3 in the hydrolysis of hemoglobin
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-
?
EDANS-CO-CH2-CH2-CO-Ala-Leu-Glu-Arg-Met-Phe-Leu-Ser-Phe-Pro-Dap-(DABCYL)-OH + H2O
?
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-
-
-
?
Lys-Pro-Ile-Gln-Phe-4-nitrophenylalanine-Arg-Leu + H2O
Lys-Pro-Ile-Gln-Phe + 4-nitrophenylalanine-Arg-Leu
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-
-
-
?
Lys-Pro-Ile-Glu-Phe-NO2Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + NO2Phe-Arg-Leu
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-
-
-
?
Lys-Pro-Ile-Leu-Phe-4-nitrophenylalanine-Arg-Leu + H2O
Lys-Pro-Ile-Leu-Phe + 4-nitrophenylalanine-Arg-Leu
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-
-
-
?
haemoglobin + H2O
?
human haemoglobin. At pH 4.7, the enzyme is able to degrade hemoglobin so that no bands remain visible on SDS-PAGE. When excess of hemoglobin is used a 14000 Da band is detected, consistent with a cleavage of the alpha-globin chain at the Phe33-Leu34 bond in the hinge region of the molecule
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-
?
haemoglobin + H2O
?
human haemoglobin. The enzyme may play a crucial role in the critical process which yields nutrients from parasite growth, the enzyme may have the potential to initiate the vacuolar haemoglobin digestion pathway
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-
?
Hemoglobin + H2O
?
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the enzyme is involved in host hemoglobin degradation
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-
?
Lys-Pro-Ile-Nle-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Pro-Ile-Nle-Phe + Phe(NO2)-Arg-Leu
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-
-
-
?
Lys-Pro-Ile-Nle-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Pro-Ile-Nle-Phe + Phe(NO2)-Arg-Leu
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-
-
-
?
Lys-Pro-Ile-Nle-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Pro-Ile-Nle-Phe + Phe(NO2)-Arg-Leu
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-
-
-
?
Lys-Pro-Ile-Nle-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Pro-Ile-Nle-Phe + Phe(NO2)-Arg-Leu
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-
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-
?
additional information
?
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the enzyme cleaves preferably behind phenylalanine. The hydrolysis rates of the leucine and norleucine pools are 34% and 42% of that of the phenylalanine pool, respectively. In addition, no levels of hydrolysis are also detected for peptide pools containing four other P1 amino acid substitutes, asparagine (25%), glutamine (20%), tyrosine (18%) and tryptophan (17%). Hydrolyzed peptide products from the other 12 peptide pools, however, were barely detected
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-
?
additional information
?
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-
the plasmepsin 4 zymogen exhibits catalytic activity regardless of the presence of the pro-segment. Auto-maturation of the zymogen to mature enzyme is carried out at pH 4.5, 5.0, and 5.5
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-
?
additional information
?
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since plasmepsin IV clearly can cleave within the -Ser-(Phe/Leu)-Lys-Phe-Phe-Lys-(Ser/Thr)-Gly- sequence it may be possible that plasmepsin IV initiates cleavage of the proplasmepsin I precursor
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-
?
additional information
?
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since plasmepsin IV clearly can cleave within the -Ser-(Phe/Leu)-Lys-Phe-Phe-Lys-(Ser/Thr)-Gly- sequence it may be possible that plasmepsin IV initiates cleavage of the proplasmepsin I precursor
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-
?
additional information
?
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the four plasmepsins have overlapping roles in the hemoglobin degradation pathway
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-
?
