| IED ID | IndEnz0002010888 |
| Enzyme Type ID | protease010888 |
| Protein Name |
Xaa-Pro aminopeptidase app-1 EC 3.4.11.9 Aminopeptidase P |
| Gene Name | app-1 W03G9.4 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MTALEKLAKLRSLFHSERVLALTSSKPMVAYLLPSTDAHHSEYLADYDFRVKFLSGFSGSNAYVVVTDREALLWTDGRYFTQAGNQLDSNSWKLMKQGQPDSITVVDWLVRELERGSVIGFDPTLSTFDAGSKTFKRLKAAGLQPVSIPGNLVDEFWTDRPRLAGEPVVVLDVEDTGLTTSKKVENLREKLKQKKCDAAVFTLLDDVMWLLNIRGSDIPYNPLAYSYLFVAMREIHVFIDNEKLDEKSRAHFHKSNVSIHPYGEVYSWISNWLKAKEASKEPHMVYLTPETNYAIGSIIGEENSMVDTSLVQTAKATKNDHEMQGMRNSHLRDSAALVEFLCWLEKELLSGKRYTEIELADKIDHLRSLQDKYVTLSFDTISAVGDHAALPHYKPLGESGNRKAAANQVFLLDSGAHYGDGTTDVTRTVWYTNPPKEFILHNTLVLKGHINLARAKFPDGIYGSRLDTLTRDALWKLGLDFEHGTGHGVGHYLNVHEGPIGIGHRSVPTGGELHASQVLTIEPGFYAKEKYGIRIENCYETVEAVVMSKAQNFLTFKSLTLVPIQTSIVDKSLLIEEEINWLNQYHARVLKEVGEHLQKRGKTDELKWLAEACKPI |
| Enzyme Length | 616 |
| Uniprot Accession Number | O44750 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by the metal ion chelators EDTA and 1,10-phenanthroline (PubMed:11606206). Also inhibited by apstatin (PubMed:11606206, PubMed:25905034). Activity towards bradykinin is inhibited by Mn(2+) and Zn(2+) at all concentrations tested, whereas Co(2+) is inhibitory at concentrations above 100 uM and activatory at 10 uM (PubMed:11606206). {ECO:0000269|PubMed:11606206, ECO:0000269|PubMed:25905034}. |
| Binding Site | BINDING 78; /note="Substrate"; /evidence="ECO:0000305|PubMed:25905034, ECO:0007744|PDB:4S2T"; BINDING 392; /note="Substrate; via tele nitrogen"; /evidence="ECO:0000305|PubMed:25905034, ECO:0007744|PDB:4S2T"; BINDING 487; /note="Substrate; via tele nitrogen"; /evidence="ECO:0000305|PubMed:25905034, ECO:0007744|PDB:4S2T"; BINDING 496; /note="Substrate; via tele nitrogen"; /evidence="ECO:0000305|PubMed:25905034, ECO:0007744|PDB:4S2T"; BINDING 522; /note="Substrate"; /evidence="ECO:0000305|PubMed:25905034, ECO:0007744|PDB:4S2T" |
| 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:11606206}; |
| 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 (PubMed:11606206, PubMed:25905034). Has activity towards the flp-9 neuropeptide KPSFVRF-amide (PubMed:11606206). {ECO:0000269|PubMed:11606206, ECO:0000269|PubMed:25905034}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-8. {ECO:0000269|PubMed:11606206}; |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (26); Binding site (5); Chain (1); Helix (30); Metal binding (7); Turn (5) |
| Keywords | 3D-structure;Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11606206}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 4S2R; 4S2T; |
| Mapped Pubmed ID | 10778742; 14704431; 17164286; 19343510; 19922876; 21085631; 21177967; 22267497; 22347378; 22560298; 23800452; 24884423; 25487147; 25635455; 26009280; 29348603; 6593563; |
| Motif | |
| Gene Encoded By | |
| Mass | 69,340 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=45 uM for bradykinin {ECO:0000269|PubMed:11606206}; |
| Metal Binding | METAL 413; /note="Zinc 1"; /evidence="ECO:0000269|PubMed:25905034, ECO:0007744|PDB:4S2R, ECO:0007744|PDB:4S2T"; METAL 424; /note="Zinc 1"; /evidence="ECO:0000269|PubMed:25905034, ECO:0007744|PDB:4S2R, ECO:0007744|PDB:4S2T"; METAL 424; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:25905034, ECO:0007744|PDB:4S2R, ECO:0007744|PDB:4S2T"; METAL 487; /note="Zinc 2; via tele nitrogen"; /evidence="ECO:0000269|PubMed:25905034, ECO:0007744|PDB:4S2R, ECO:0007744|PDB:4S2T"; METAL 522; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:25905034, ECO:0007744|PDB:4S2R, ECO:0007744|PDB:4S2T"; METAL 536; /note="Zinc 1"; /evidence="ECO:0000269|PubMed:25905034, ECO:0007744|PDB:4S2R, ECO:0007744|PDB:4S2T"; METAL 536; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:25905034, ECO:0007744|PDB:4S2R, ECO:0007744|PDB:4S2T" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.9; |