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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: O60990
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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, ppm iv, pgpm4, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A01.059
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PfPM4
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plasmepsin 4
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
429673-77-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O60990_PLAMA
451
0
51809
TrEMBL
other Location (Reliability: 2)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
pKa calculations for PM IV complexed with the inhibitor KNI-764. Residue Asp214 is protonated, while residue Asp34 is deprotonated. In the colmplex, the hydroxyl group interacts with the OD2 oxygen atom of Asp34 through a hydrogen bond. The hydroxyl group also presents a hydrogen bond interaction with acid aspartic protonated Asp214. The amino groups of Gly78 and Ser79 residues interact with KNI-764 forming hydrogen bonds at 2.02 and 2.20 A. The hydroxyl group of Thr217 forms hydrogen bonds with the inhibitor at 2.06 A
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Silva, N.; Lameira, J.; Alves, C.
A quantum mechanical/molecular mechanical study of the aspartic protease plasmepsin IV complexed with allophenylnorstatine-based inhibitor
Chem. Phys. Lett.
509
169-174
2011
Plasmodium malariae (O60990)
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Manually annotated by BRENDA team