| IED ID | IndEnz0002010891 |
| Enzyme Type ID | protease010891 |
| Protein Name |
Xaa-Pro aminopeptidase ApepP EC 3.4.11.9 Aminopeptidase P AP-P |
| Gene Name | ApepP CG6291 |
| Organism | Drosophila melanogaster (Fruit fly) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly) |
| Enzyme Sequence | MKRSTTQILTRLRELMLRAQVGDSCGISAYIVPSDDAHQSEYQCQHDERRSFVSGFDGSAGTAVITTETALLWTDGRYYQQAEKQLDSNWVLMRDGLSATPSIGAWLAKNLPKGSFVGVDPRLLSFRVWKPIETELSSAECQLVPIEGNLIDEVWGEDQPPQTSNKIITLKLEHSGVTIAKKWDVVRQQLKEKNADALVVSALDEIAWFLNLRGSDIDFNPVFFSYLIVTNDELLLFVDSGKLPTDFVQHQKENNVQISVLPYASIGIEISKIVSTRESKIWIAPTSSYYLTALIPKSRRIQEVTPICVLKAIKNDVEIAGFINSHIRDGVALCQYFAWLEDQVNKGAEVDEMSGADKLESFRSTKDKYMGLSFTTISASGPNGSVIHYHPKKETNRKINDKEIYLCDSGAQYLDGTTDVTRTLHFGEPTEFQKEAYTRVLKGQLSFGSTVFPAKVKGQVLDTLARKALWDVGLDYGHGTGHGVGHFLNVHEGPMGVGIRLMPDDPGLQANMFISNEPGFYQDGEFGIRVEDIVQIVPGQVAHNFSNRGALTFKTITMCPKQTKMIKKELLSDAEVKLLNSYHQQVWDTLSPILSREGDEFTLSWLKKEVQPI |
| Enzyme Length | 613 |
| Uniprot Accession Number | Q9VJG0 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the chelating agent EDTA. Divalent metal ions have substrate- and concentration-dependent effects on activity. Activity towards bradykinin is inhibited with increasing Mn(2+) concentration. Activity towards substance P is stimulated by low Mn(2+) concentrations (in the range 10 uM-1 mM) but inhibited by Mn(2+) concentrations in excess of 1 mM. Ca(2+), Mg(2+) and Co(2+) stimulate activity towards substance P at concentrations of 10-100 uM but are inhibitory at concentrations of 1 mM. Zn(2+), Ni(2+) and Cu(2+) strongly inhibit activity towards substance P at concentrations of 1 mM. {ECO:0000269|PubMed:11872174}. |
| Binding Site | BINDING 77; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 388; /note=Substrate; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 482; /note=Substrate; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 491; /note=Substrate; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 517; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O44750 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.; EC=3.4.11.9; Evidence={ECO:0000269|PubMed:11872174}; |
| DNA Binding | |
| EC Number | 3.4.11.9 |
| Enzyme Function | FUNCTION: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. {ECO:0000269|PubMed:11872174}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.6. {ECO:0000269|PubMed:11872174}; |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (5); Chain (1); Metal binding (7) |
| Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Manganese;Metal-binding;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11872174}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11819115; 12865422; 14630943; 14711877; 17785192; 18931788; 19640479; 21960044; 23071443; 23944235; 26290570; 26526100; 26700685; 26870755; 27287809; 31722958; |
| Motif | |
| Gene Encoded By | |
| Mass | 68,506 |
| Kinetics | |
| Metal Binding | METAL 408; /note=Manganese 1; /evidence=ECO:0000250|UniProtKB:Q9NQW7; METAL 419; /note=Manganese 1; /evidence=ECO:0000250|UniProtKB:Q9NQW7; METAL 419; /note=Manganese 2; /evidence=ECO:0000250|UniProtKB:Q9NQW7; METAL 482; /note=Manganese 2; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q9NQW7; METAL 517; /note=Manganese 2; /evidence=ECO:0000250|UniProtKB:Q9NQW7; METAL 531; /note=Manganese 1; /evidence=ECO:0000250|UniProtKB:Q9NQW7; METAL 531; /note=Manganese 2; /evidence=ECO:0000250|UniProtKB:Q9NQW7 |
| Rhea ID | |
| Cross Reference Brenda |