| IED ID | IndEnz0002011821 |
| Enzyme Type ID | protease011821 |
| Protein Name |
Xaa-Pro aminopeptidase 2 EC 3.4.11.9 Aminoacylproline aminopeptidase Membrane-bound aminopeptidase P Membrane-bound APP Membrane-bound AmP mAmP X-Pro aminopeptidase 2 |
| Gene Name | XPNPEP2 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MARAHWGCCPWLVLLCACAWGHTKPVDLGGQDVRNCSTNPPYLPVTVVNTTMSLTALRQQMQTQNLSAYIIPGTDAHMNEYIGQHDERRAWITGFTGSAGTAVVTMKKAAVWTDSRYWTQAERQMDCNWELHKEVGTTPIVTWLLTEIPAGGRVGFDPFLLSIDTWESYDLALQGSNRQLVSITTNLVDLVWGSERPPVPNQPIYALQEAFTGSTWQEKVSGVRSQMQKHQKVPTAVLLSALEETAWLFNLRASDIPYNPFFYSYTLLTDSSIRLFANKSRFSSETLSYLNSSCTGPMCVQIEDYSQVRDSIQAYSLGDVRIWIGTSYTMYGIYEMIPKEKLVTDTYSPVMMTKAVKNSKEQALLKASHVRDAVAVIRYLVWLEKNVPKGTVDEFSGAEIVDKFRGEEQFSSGPSFETISASGLNAALAHYSPTKELNRKLSSDEMYLLDSGGQYWDGTTDITRTVHWGTPSAFQKEAYTRVLIGNIDLSRLIFPAATSGRMVEAFARRALWDAGLNYGHGTGHGIGNFLCVHEWPVGFQSNNIAMAKGMFTSIEPGYYKDGEFGIRLEDVALVVEAKTKYPGSYLTFEVVSFVPYDRNLIDVSLLSPEHLQYLNRYYQTIREKVGPELQRRQLLEEFEWLQQHTEPLAARAPDTASWASVLVVSTLAILGWSV |
| Enzyme Length | 674 |
| Uniprot Accession Number | O43895 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by apstatin and the chelating agent 1,10-phenanthroline. Also inhibited by high concentrations of Zn(2+). Not significantly inhibited by bestatin or phosphoramidon. {ECO:0000269|PubMed:15361070}. |
| Binding Site | BINDING 116; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 430; /note=Substrate; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 524; /note=Substrate; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 533; /note=Substrate; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 555; /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:15361070}; |
| DNA Binding | |
| EC Number | 3.4.11.9 |
| Enzyme Function | FUNCTION: Membrane-bound metalloprotease which catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. May play a role in the metabolism of the vasodilator bradykinin. {ECO:0000269|PubMed:15361070}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4. {ECO:0000269|PubMed:15361070}; |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (5); Chain (1); Glycosylation (5); Lipidation (1); Metal binding (7); Natural variant (3); Propeptide (1); Sequence conflict (2); Signal peptide (1) |
| Keywords | Aminopeptidase;Cell membrane;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q95333}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q95333}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:15361070}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11072085; 17003818; 18158172; 18515364; 19178938; 21052031; 23276181; 2443973; 27788882; 28670957; 31296901; 3422494; |
| Motif | |
| Gene Encoded By | |
| Mass | 75,625 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.837 mM for Arg-Pro-Pro {ECO:0000269|PubMed:15361070}; KM=75 uM for Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg (bradykinin) {ECO:0000269|PubMed:15361070}; KM=56 uM for Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe (bradykinin[1-8]) {ECO:0000269|PubMed:15361070}; KM=18 uM for synthetic fluorescent substrate Lys(Dnp)-Pro-Pro-Gly-Phe-Ser-Pro-Lys(Abz)NH(2) {ECO:0000269|PubMed:15361070}; KM=20 uM for synthetic fluorescent substrate Lys(Dnp)-Pro-Pro-Gly-Lys(Abz)NH(2) {ECO:0000269|PubMed:15361070}; KM=19 uM for synthetic fluorescent substrate Lys(Dnp)-Pro-Pro-Lys(Abz)NH(2) {ECO:0000269|PubMed:15361070}; |
| Metal Binding | METAL 450; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:O44750; METAL 461; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:O44750; METAL 461; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:O44750; METAL 524; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:O44750; METAL 555; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:O44750; METAL 569; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:O44750; METAL 569; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:O44750 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.9; |