| IED ID | IndEnz0002005708 |
| Enzyme Type ID | protease005708 |
| Protein Name |
Aspartyl aminopeptidase EC 3.4.11.21 |
| Gene Name | DNPEP ASPEP DAP |
| 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 | MSGHSPTRGAMQVAMNGKARKEAVQTAAKELLKFVNRSPSPFHAVAECRNRLLQAGFSELKETEKWNIKPESKYFMTRNSSTIIAFAVGGQYVPGNGFSLIGAHTDSPCLRVKRRSRRSQVGFQQVGVETYGGGIWSTWFDRDLTLAGRVIVKCPTSGRLEQQLVHVERPILRIPHLAIHLQRNINENFGPNTEMHLVPILATAIQEELEKGTPEPGPLNAVDERHHSVLMSLLCAHLGLSPKDIVEMELCLADTQPAVLGGAYDEFIFAPRLDNLHSCFCALQALIDSCAGPGSLATEPHVRMVTLYDNEEVGSESAQGAQSLLTELVLRRISASCQHPTAFEEAIPKSFMISADMAHAVHPNYLDKHEENHRPLFHKGPVIKVNSKQRYASNAVSEALIREVANKVKVPLQDLMVRNDTPCGTTIGPILASRLGLRVLDLGSPQLAMHSIREMACTTGVLQTLTLFKGFFELFPSLSHNLLVD |
| Enzyme Length | 485 |
| Uniprot Accession Number | Q9ULA0 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: One of the zinc ions is readily exchangeable with other divalent cations such as manganese, which strongly stimulates the enzymatic activity. {ECO:0000250}. |
| Binding Site | BINDING 180; /note=Substrate; /evidence=ECO:0000269|PubMed:22720794; BINDING 311; /note=Substrate; /evidence=ECO:0000269|PubMed:22720794; BINDING 356; /note=Substrate; /evidence=ECO:0000269|PubMed:22720794; BINDING 359; /note=Substrate; /evidence=ECO:0000269|PubMed:22720794; BINDING 384; /note=Substrate; /evidence=ECO:0000269|PubMed:22720794; BINDING 391; /note=Substrate; /evidence=ECO:0000269|PubMed:22720794 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate.; EC=3.4.11.21; Evidence={ECO:0000269|PubMed:9632644}; |
| DNA Binding | |
| EC Number | 3.4.11.21 |
| Enzyme Function | FUNCTION: Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism. {ECO:0000269|PubMed:9632644}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Beta strand (18); Binding site (6); Chain (1); Erroneous initiation (2); Frameshift (1); Helix (16); Metal binding (6); Modified residue (2); Sequence conflict (2); Turn (7) |
| Keywords | 3D-structure;Acetylation;Alternative initiation;Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;Zinc |
| Interact With | Itself; Q8TBB1; Q00013 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9632644}. |
| Modified Residue | MOD_RES 213; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:24275569; MOD_RES Q9ULA0-2:1; /note=N-acetylmethionine; /evidence=ECO:0007744|PubMed:22814378 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4DYO; |
| Mapped Pubmed ID | 12413488; 16189514; 17353931; 23948443; 25416956; 25525879; 31228326; |
| Motif | |
| Gene Encoded By | |
| Mass | 53,410 |
| Kinetics | |
| Metal Binding | METAL 104; /note=Zinc 1; /evidence=ECO:0000269|PubMed:22720794; METAL 274; /note=Zinc 1; /evidence=ECO:0000269|PubMed:22720794; METAL 274; /note=Zinc 2; /evidence=ECO:0000269|PubMed:22720794; METAL 312; /note=Zinc 2; /evidence=ECO:0000269|PubMed:22720794; METAL 356; /note=Zinc 1; /evidence=ECO:0000269|PubMed:22720794; METAL 450; /note=Zinc 2; /evidence=ECO:0000269|PubMed:22720794 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.21; |