| IED ID | IndEnz0002010512 |
| Enzyme Type ID | protease010512 |
| Protein Name |
Prolyl endopeptidase PE EC 3.4.21.26 POase Post-proline cleaving enzyme |
| Gene Name | prep dpoA DDB_G0274387 |
| Organism | Dictyostelium discoideum (Slime mold) |
| Taxonomic Lineage | cellular organisms Eukaryota Amoebozoa Evosea Eumycetozoa Dictyostelia (dictyostelid cellular slime molds) Dictyosteliales Dictyosteliaceae Dictyostelium Dictyostelium discoideum (Slime mold) |
| Enzyme Sequence | MKFNYPETRRDDSVFDIFKSTEKGSVKVYDPYRHLEDQQSPETKKWVDEENKITRSFLDQDNTSEKISNEIMKMLNFERFDWFRRRGSKLFFSRNPNTLNQNIIYLIDIDQISISKDGKSSAKGFENAIEFLNPNTYSKDGTWSLKSFVISKSGDHVCFSYSKAGSDWEEIAVKKIITTNELKTNKDDEEEKEDLKKKNCLHYAVVDLPDSINWCKFTSIKWDENETGFIYNRYPKPEKVSDDDKGTETDTNLNNKVYYHKLGDANESFDRVVFECPENPQWIFGTEFSHDHSSLFISAFRDCNVEHNLYVIRNFQEAIANKSAFKVEALIDNFDACYYYITNTKQGEYFFLTNLSAPFNRLISIQLNDDQPIVPNSKSKLEFKEIIPEKDYVLESVSRSSQEKFYVSYQKHVQDIIEVYDFNGKYLKDIKLPGPGSASLSATEYHDHIFINFSNLVSPSVTYYMDSKNDELLLFKEPHIEGFKSSDYECKQVFYESPKDKTKIPMFIAYKKTTDITSGNAPTYMTGYGGFNISYTQSFSIRNIYFLNKFNGIFVIANIRGGGEYGKAWHEAGSKKNKQNCFDDFIGAAEYLIKENYTNQNKLAVRGGSNGGLLMGAISNQRPDLFKCVVADVGVMDMLRFHLHTIGSNWVSDYGRSDNPDDFDVLIKYSPLNNVPKDSNQYPSIMLCTGDHDDRVIPAHSYKFISELQYQLGKKVDTPLLIRVDKDSGHGAGKGLSKQNNEIADIFNFFSKVLNVKLNF |
| Enzyme Length | 760 |
| Uniprot Accession Number | Q86AS5 |
| Absorption | |
| Active Site | ACT_SITE 609; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10084; ACT_SITE 693; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10084; ACT_SITE 730; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10084 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by chymostatin, Boc-Glu(NHO-Bz)-Pyrrolidide, Z-Pro-L-prolinal dimethyacetal and the peptide H-H-L-P-P-P-V-OH. {ECO:0000269|PubMed:10329620}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.; EC=3.4.21.26; |
| DNA Binding | |
| EC Number | 3.4.21.26 |
| Enzyme Function | FUNCTION: Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Sequence conflict (6) |
| Keywords | Cytoplasm;Hydrolase;Protease;Reference proteome;Serine protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10329620}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15950352; 16890490; 18590548; 21093602; 21222625; |
| Motif | |
| Gene Encoded By | |
| Mass | 87,555 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=115 uM for carbobenzoxy-Gly-Pro-p-nitroanilide (at 37 degrees Celsius) {ECO:0000269|PubMed:10329620}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |