| IED ID | IndEnz0002012672 |
| Enzyme Type ID | protease012672 |
| Protein Name |
Xaa-Pro aminopeptidase 1 EC 3.4.11.9 Aminoacylproline aminopeptidase Cytosolic aminopeptidase P Soluble aminopeptidase P sAmp X-Pro aminopeptidase 1 X-prolyl aminopeptidase 1, soluble |
| Gene Name | XPNPEP1 XPNPEPL XPNPEPL1 |
| 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 | MPPKVTSELLRQLRQAMRNSEYVTEPIQAYIIPSGDAHQSEYIAPCDCRRAFVSGFDGSAGTAIITEEHAAMWTDGRYFLQAAKQMDSNWTLMKMGLKDTPTQEDWLVSVLPEGSRVGVDPLIIPTDYWKKMAKVLRSAGHHLIPVKENLVDKIWTDRPERPCKPLLTLGLDYTGISWKDKVADLRLKMAERNVMWFVVTALDEIAWLFNLRGSDVEHNPVFFSYAIIGLETIMLFIDGDRIDAPSVKEHLLLDLGLEAEYRIQVHPYKSILSELKALCADLSPREKVWVSDKASYAVSETIPKDHRCCMPYTPICIAKAVKNSAESEGMRRAHIKDAVALCELFNWLEKEVPKGGVTEISAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPVPETNRTLSLDEVYLIDSGAQYKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSFARSALWDSGLDYLHGTGHGVGSFLNVHEGPCGISYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPVKTKYNFNNRGSLTFEPLTLVPIQTKMIDVDSLTDKECDWLNNYHLTCRDVIGKELQKQGRQEALEWLIRETQPISKQH |
| Enzyme Length | 623 |
| Uniprot Accession Number | Q9NQW7 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by apstatin and the metal ion chelators EDTA and 1,10-phenanthroline. Partially inhibited by dithiothreitol. Not inhibited by enalaprilat or amastatin. {ECO:0000269|PubMed:11106490}. |
| Binding Site | BINDING 77; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 395; /note=Substrate; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 489; /note=Substrate; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 498; /note=Substrate; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 523; /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:11106490, ECO:0000269|PubMed:18515364}; |
| DNA Binding | |
| EC Number | 3.4.11.9 |
| Enzyme Function | FUNCTION: Contributes to the degradation of bradykinin. Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.2. {ECO:0000269|PubMed:11106490, ECO:0000269|PubMed:18515364}; |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Beta strand (26); Binding site (5); Chain (1); Erroneous initiation (1); Helix (32); Initiator methionine (1); Metal binding (7); Modified residue (1); Mutagenesis (2); Sequence conflict (7); Turn (4) |
| Keywords | 3D-structure;Acetylation;Alternative splicing;Aminopeptidase;Cytoplasm;Direct protein sequencing;Hydrolase;Manganese;Metal-binding;Metalloprotease;Protease;Reference proteome |
| Interact With | Q96D03; Q9H8Y8; P69892; Q15669 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
| Modified Residue | MOD_RES 304; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:19608861 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3CTZ; |
| Mapped Pubmed ID | 16169070; 16385451; 17043677; 19126663; 20379614; 20460270; 21052031; 21900206; 29351301; |
| Motif | |
| Gene Encoded By | |
| Mass | 69,918 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=100.6 uM for bradykinin {ECO:0000269|PubMed:11106490, ECO:0000269|PubMed:18515364}; KM=308 uM for the tripeptide Arg-Pro-Pro {ECO:0000269|PubMed:11106490, ECO:0000269|PubMed:18515364}; |
| Metal Binding | METAL 415; /note="Manganese 1"; /evidence="ECO:0000269|PubMed:18515364, ECO:0007744|PDB:3CTZ"; METAL 426; /note="Manganese 1"; /evidence="ECO:0000269|PubMed:18515364, ECO:0007744|PDB:3CTZ"; METAL 426; /note="Manganese 2"; /evidence="ECO:0000269|PubMed:18515364, ECO:0007744|PDB:3CTZ"; METAL 489; /note="Manganese 2; via tele nitrogen"; /evidence="ECO:0000269|PubMed:18515364, ECO:0007744|PDB:3CTZ"; METAL 523; /note="Manganese 2"; /evidence="ECO:0000269|PubMed:18515364, ECO:0007744|PDB:3CTZ"; METAL 537; /note="Manganese 1"; /evidence="ECO:0000269|PubMed:18515364, ECO:0007744|PDB:3CTZ"; METAL 537; /note="Manganese 2"; /evidence="ECO:0000269|PubMed:18515364, ECO:0007744|PDB:3CTZ" |
| Rhea ID | |
| Cross Reference Brenda | 3.1.8.1;3.4.11.9; |