| IED ID | IndEnz0002006243 |
| Enzyme Type ID | protease006243 |
| Protein Name |
Protein DDI1 homolog EC 3.4.23.- DDI1-like protein |
| Gene Name | DDI1 |
| Organism | Leishmania major |
| Taxonomic Lineage | cellular organisms Eukaryota Discoba Euglenozoa Kinetoplastea (kinetoplasts) Metakinetoplastina Trypanosomatida Trypanosomatidae Leishmaniinae Leishmania Leishmania Leishmania major species complex Leishmania major |
| Enzyme Sequence | MVQLTIDNARGVTLCRVSLPANATVQQLLLQLTVAKPELRQAQAIRNDVRHVTHRLTPASTTTTTTTSVVSSNAQTLLQAGLVGQGATAETLVVLMAADAPAAASSAAAAAPSPTKAVAAQILDLFGCASASPSAGVRSQASVVPSTMDERQLELQRRIYAQIQQQQIDENLANALEYTPEAFAKVTMLYVPCTINQVLVKAFVDSGAQNSIMNKRTAERCGLMRLVDVRMRDVAVGVGRQEICGRIHMTPVNLAGMYIPFAFYVIEDQAMDLIIGLDQLKRHQMMIDLKHNCLTIDNINVPFLPENDLPALAALGDDENAMHAPRHQDPATTATTASNPAAPVLSEGERQARIEGFMTVSGITDPTQAAELLEAADWNPNVAAALLFDT |
| Enzyme Length | 390 |
| Uniprot Accession Number | I7HUG0 |
| Absorption | |
| Active Site | ACT_SITE 205; /evidence=ECO:0000305 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by pepstatin, diazoacetyl-DL-norleucine methyl ester (DAN) and nelfinavir (PubMed:22933181). Inhibited by the proteinase inhibitors lopinavir and ritonavir (PubMed:21266539). {ECO:0000269|PubMed:21266539, ECO:0000269|PubMed:22933181}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.23.- |
| Enzyme Function | FUNCTION: Aspartic protease (PubMed:22933181, PubMed:21266539). {ECO:0000269|PubMed:22933181, ECO:0000305|PubMed:21266539}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5 with RE-(EDANS)-SQNYPIVQK-(DABCYL)-R as substrate. {ECO:0000269|PubMed:22933181}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (10); Chain (1); Helix (4); Mutagenesis (1); Region (1); Turn (3) |
| Keywords | 3D-structure;Aspartyl protease;Cytoplasm;Hydrolase;Protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40087}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 5YQ8; 5YS4; |
| Mapped Pubmed ID | 30186740; |
| Motif | |
| Gene Encoded By | |
| Mass | 41,744 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.57 uM for RE-(EDANS)-SQNYPIVQK-(DABCYL)-R (at 37 degrees Celsius and pH 4-6.5) {ECO:0000269|PubMed:22933181}; KM=7.6 uM for Bz-RGFFL-4MbetaNA (at 37 degrees Celsius and pH 4) {ECO:0000269|PubMed:22933181}; KM=1.18 uM for Bz-RGFFP-4MbetaNA (at 37 degrees Celsius and pH 8) {ECO:0000269|PubMed:22933181}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |