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Information on EC 3.4.23.B14 - plasmepsin IV

for references in articles please use BRENDA:EC3.4.23.B14
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.B14 plasmepsin IV
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This record set is specific for:
UNIPROT: O60989
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Word Map
The expected taxonomic range for this enzyme is: Plasmodium
Reaction Schemes
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.
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
plasmepsin 4, pvpm4, plasmepsin iv, plm iv, pm iv, pfpm4, pmpm4, pm-iv, pgpm4, ppm iv, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
plasmepsin 4
-
A01.059
-
-
-
-
PfPM4
-
-
-
-
plasmepsin 4
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
429673-77-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
denatured human hemoglobin + H2O
?
show the reaction diagram
preferred over native human hemoglobin. PvPM4 acts synergistically with cysteine proteases vivapain-2 and vivapain-3 in the hydrolysis of hemoglobin
-
-
?
native human gemoglobin + H2O
?
show the reaction diagram
poor substrate
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pepstatin
efficinet inhibition of autoprocessing to mature PM4
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 5.5
broad
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O60989_PLAVI
450
0
51667
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
x * 44000, SDs-PAGE of preprotein, x * 37000, SDS-PAGE of mature protein
44000
x * 44000, SDs-PAGE of preprotein, x * 37000, SDS-PAGE of mature protein
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 44000, SDs-PAGE of preprotein, x * 37000, SDS-PAGE of mature protein
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
processing of PM4 into a mature enzyme occurrs through autocatalytic activity under acidic conditions in a pepstatin A-sensitive manner, in which process a portion of prodomain is essential for correct folding. Cysteine proteases vivapain-2 and vivapain-3 mediate the processing of PvPM4 into a mature enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
highly stable under acidic and neutral conditions
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
bacterially expressed recombinant PvPM4 is insoluble, but it is easily refolded into a soluble protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Moon, S.U.; Kang, J.M.; Kim, T.S.; Kong, Y.; Sohn, W.M.; Na, B.K.
Plasmodium vivax: collaborative roles for plasmepsin 4 and vivapains in hemoglobin hydrolysis
Exp. Parasitol.
128
127-132
2011
Plasmodium vivax (O60989), Plasmodium vivax
Manually annotated by BRENDA team