| IED ID | IndEnz0002000953 |
| Enzyme Type ID | protease000953 |
| Protein Name |
Plasmepsin III EC 3.4.23.39 Histo-aspartic protease PfHAP Plasmepsin 3 |
| Gene Name | PMIII HAP PF3D7_1408100 |
| 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 | MNLTIKEEDFTNTFMKNEESFNTFRVTKVKRWNAKRLFKILFVTVFIVLAGGFSYYIFENFVFQKNRKINHIIKTSKYSTVGFNIENSYDRLMKTIKEHKLKNYIKESVKLFNKGLTKKSYLGSEFDNVELKDLANVLSFGEAKLGDNGQKFNFLFHTASSNVWVPSIKCTSESCESKNHYDSSKSKTYEKDDTPVKLTSKAGTISGIFSKDLVTIGKLSVPYKFIEMTEIVGFEPFYSESDVDGVFGLGWKDLSIGSIDPYIVELKTQNKIEQAVYSIYLPPENKNKGYLTIGGIEERFFDGPLNYEKLNHDLMWQVDLDVHFGNVSSKKANVILDSATSVITVPTEFFNQFVESASVFKVPFLSLYVTTCGNTKLPTLEYRSPNKVYTLEPKQYLEPLENIFSALCMLNIVPIDLEKNTFVLGDPFMRKYFTVYDYDNHTVGFALAKNL |
| Enzyme Length | 451 |
| Uniprot Accession Number | Q8IM15 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Dimerization causes loss of catalytic activity (PubMed:20435072). Inhibited by pepstatin A (PubMed:16624575). Inhibited by Zn(2+) (PubMed:20435072). {ECO:0000269|PubMed:16624575, ECO:0000269|PubMed:20435072}. |
| 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:16624575, ECO:0000269|PubMed:18312598, ECO:0000269|PubMed:20435072}; |
| 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:16624575). 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:16624575, ECO:0000305}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.2 (PubMed:16624575). Activity decreases sharply at pH above 6 (PubMed:16624575). Optimum pH is 5.5-7.5 (PubMed:18312598). {ECO:0000269|PubMed:16624575, ECO:0000269|PubMed:18312598}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (2); Domain (1); Mutagenesis (3); 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:0000305}. 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 (By similarity). Proteolysis requires an acidic environment (By similarity). Transprocessing may serve as an alternate activation system (PubMed:18312598). {ECO:0000250|UniProtKB:P39898, ECO:0000250|UniProtKB:Q9Y006, ECO:0000269|PubMed:18312598}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 3FNS; 3FNT; 3FNU; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 51,693 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |