| IED ID | IndEnz0002007456 |
| Enzyme Type ID | protease007456 |
| Protein Name |
Plasmepsin IV EC 3.4.23.39 Plasmepsin 4 |
| Gene Name | PMIV PF3D7_1407800 |
| Organism | Plasmodium falciparum (isolate 3D7) |
| Taxonomic Lineage | cellular organisms Eukaryota Sar Alveolata Apicomplexa Aconoidasida Haemosporida (haemosporidians) Plasmodiidae Plasmodium Plasmodium (Laverania) Plasmodium falciparum Plasmodium falciparum (isolate 3D7) |
| Enzyme Sequence | MALTVKEEEFSNTLIKNASAFDRLKLGNLKNLKIQKKLQFLYLILFVLITGVFFFFLIGNFYSHRKLYQVIKNTKHTTIGFKIDRPHDKVLSSVLKNKLSTYVKESFKFFKSGYAQKGYLGSENDSIELDDVANLMFYGEGQIGTNKQPFMFIFDTGSANLWVPSVNCDSIGCSTKHLYDASASKSYEKDGTKVEISYGSGTVRGYFSKDVISLGDLSLPYKFIEVTDADDLEPIYSGSEFDGILGLGWKDLSIGSIDPVVVELKKQNKIDNALFTFYLPVHDKHVGYLTIGGIESDFYEGPLTYEKLNHDLYWQIDLDIHFGKYVMQKANAVVDSGTSTITAPTSFLNKFFRDMNVIKVPFLPLYVTTCDNDDLPTLEFHSRNNKYTLEPEFYMDPLSDIDPALCMLYILPVDIDDNTFILGDPFMRKYFTVFDYEKESVGFAVAKNL |
| Enzyme Length | 449 |
| Uniprot Accession Number | Q8IM16 |
| 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 KNI derived compounds KNI-10333 and to a lesser extent KNI-10743. {ECO:0000269|PubMed:29943906}. |
| 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:29943906}; |
| DNA Binding | |
| EC Number | 3.4.23.39 |
| Enzyme Function | FUNCTION: During the asexual blood stage, catalyzes the cleavage of denatured host hemoglobin (Hb) (By similarity). Digestion of host Hb is an essential step which provides the parasite with amino acids for protein synthesis, and regulates osmolarity (Probable). {ECO:0000250|UniProtKB:Q17SB3, ECO:0000305}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (2); Domain (1); Propeptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | 3D-structure;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:0000255}. Vacuole lumen {ECO:0000269|PubMed:23471987}. Note=In trophozoites, localizes to the digestive (or food) vacuole, an acidic vacuole where host hemoglobin is digested. {ECO:0000269|PubMed:23471987}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically cleaved into the soluble active mature form by cysteine proteases in the digestive vacuole of trophozoites. Proteolysis requires an acidic environment. Autoprocessing or transprocessing by other plasmepsins such as PMII may serve as an alternate activation system. {ECO:0000250|UniProtKB:Q17SB3}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1LS5; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 51,046 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.23.B14; |