| IED ID | IndEnz0002007366 |
| Enzyme Type ID | protease007366 |
| Protein Name |
Plasmepsin IV EC 3.4.23.39 Plasmepsin 4 |
| Gene Name | PMIV PFHG_00463 |
| Organism | Plasmodium falciparum (isolate HB3) |
| Taxonomic Lineage | cellular organisms Eukaryota Sar Alveolata Apicomplexa Aconoidasida Haemosporida (haemosporidians) Plasmodiidae Plasmodium Plasmodium (Laverania) Plasmodium falciparum Plasmodium falciparum (isolate HB3) |
| Enzyme Sequence | MALTVKEEEFSNTLIKNASAFDRLKLGNLKNLKIQKKLQFLYLILFVLITGVFFFFLIGNFYSHRKLYQVIKNTKHTTIGFKIDRPHDKVLSSVLKNKLSTYVKESFKFFKSGYAQKGYLGSENDSIELDDVANLMFYGEGQIGTNKQPFMFIFDTGSANLWVPSVNCDSIGCSTKHLYDASASKSYEKDGTKVEISYGSGTVRGYFSKDVISLGDLSLPYKFIEVTDADDLEPIYSGSEFDGILGLGWKDLSIGSIDPVVVELKKQNKIDNALFTFYLPVHDKHVGYLTIGGIESDFYEGPLTYEKLNHDLYWQIDLDIHFGKYVMQKANAVVDSGTSTITAPTSFLNKFFTDMNVIKVPFLPLYVTTCDNDDLPTLEFHSRNNKYTLEPEFYMDPLSDIDPALCMLYILPVDIDDNTFILGDPFMRKYFTVFDYEKESVGFAVAKNL |
| Enzyme Length | 449 |
| Uniprot Accession Number | Q17SB3 |
| Absorption | |
| Active Site | ACT_SITE 155; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103; ACT_SITE 335; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by pepstatin A. {ECO:0000269|PubMed:11782538, ECO:0000269|PubMed:16452306}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of the bonds linking certain hydrophobic residues in hemoglobin or globin. Also cleaves small molecules substrates such as Ala-Leu-Glu-Arg-Thr-Phe-|-Phe(NO(2))-Ser-Phe-Pro-Thr.; EC=3.4.23.39; Evidence={ECO:0000269|PubMed:11782538, ECO:0000269|PubMed:16452306}; |
| DNA Binding | |
| EC Number | 3.4.23.39 |
| Enzyme Function | FUNCTION: During the asexual blood stage, catalyzes the cleavage of denatured host hemoglobin (Hb) or globins (PubMed:11782538, PubMed:16452306). Digestion of host Hb is an essential step which provides the parasite with amino acids for protein synthesis, and regulates osmolarity (Probable). {ECO:0000269|PubMed:11782538, ECO:0000269|PubMed:16452306, ECO:0000305}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.4. {ECO:0000269|PubMed:11782538}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (2); Domain (1); Erroneous gene model prediction (1); Mutagenesis (2); Propeptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | Aspartyl protease;Disulfide bond;Hydrolase;Membrane;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Vacuole;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}. Vacuole lumen {ECO:0000269|PubMed:11782538, ECO:0000269|PubMed:12850260}. Note=In trophozoites, localizes to the digestive (or food) vacuole, an acidic vacuole where host hemoglobin is digested. {ECO:0000269|PubMed:11782538, ECO:0000269|PubMed:12850260}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically cleaved into the soluble active mature form by cysteine proteases in the digestive vacuole of trophozoites (Probable). Proteolysis requires an acidic environment (Probable) (PubMed:16452306). Autoprocessing or transprocessing by other plasmepsins such as PMII may serve as an alternate activation system (PubMed:16452306). {ECO:0000269|PubMed:16452306, ECO:0000305|PubMed:11782538, ECO:0000305|PubMed:12850260}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 50,991 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |