| IED ID | IndEnz0002005834 |
| Enzyme Type ID | protease005834 |
| Protein Name |
Aspartyl aminopeptidase EC 3.4.11.21 |
| Gene Name | DNPEP |
| Organism | Bos taurus (Bovine) |
| 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 Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine) |
| Enzyme Sequence | MSGRARKEAVQAAARELLKFVNRSPSPFHAVAECRSRLLQAGFHELKETESWDIKPESKYFLTRNSSTIIAFAVGGQYVPGNGFSLIGAHTDSPCLRVKRRSRRSQVGFQQVGVETYGGGIWSTWFDRDLTLAGRVIVKCPTSGRLEQRLVHVDRPILRIPHLAIHLQRNVNENFGPNMEMHLVPILATSIQEELEKGTPEPGPLNATDERHHSVLTSLLCAHLGLSPEDILEMELCLADTQPAVLGGAYEEFIFAPRLDNLHSCFCALQALIDSCSAPASLAADPHVRMIALYDNEEVGSESAQGAQSLLTELVLRRISASPQHLTAFEEAIPKSYMISADMAHAVHPNYLDKHEENHRPLFHKGPVIKVNSKQRYASNAVSEALIREVASSVGVPLQDLMVRNDSPCGTTIGPILASRLGLRVLDLGSPQLAMHSIRETACTTGVLQTITLFKGFFELFPSLSRSLLVD |
| Enzyme Length | 471 |
| Uniprot Accession Number | Q2HJH1 |
| 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:0000269|PubMed:22356908}. |
| Binding Site | BINDING 166; /note=Substrate; /evidence=ECO:0000250; BINDING 297; /note=Substrate; /evidence=ECO:0000250; BINDING 342; /note=Substrate; /evidence=ECO:0000250; BINDING 345; /note=Substrate; /evidence=ECO:0000250; BINDING 370; /note=Substrate; /evidence=ECO:0000250; BINDING 377; /note=Substrate; /evidence=ECO:0000250 |
| 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; |
| 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 (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (19); Binding site (6); Chain (1); Helix (17); Metal binding (6); Modified residue (1); Turn (6) |
| Keywords | 3D-structure;Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | MOD_RES 199; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q9ULA0 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 3VAR; 3VAT; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 51,828 |
| Kinetics | |
| Metal Binding | METAL 90; /note=Zinc 1; METAL 260; /note=Zinc 1; METAL 260; /note=Zinc 2; METAL 298; /note=Zinc 2; METAL 342; /note=Zinc 1; METAL 436; /note=Zinc 2 |
| Rhea ID | |
| Cross Reference Brenda |