| IED ID | IndEnz0002000208 |
| Enzyme Type ID | protease000208 |
| Protein Name |
Probable alpha-aspartyl dipeptidase EC 3.4.13.21 Asp-specific dipeptidase Dipeptidase E |
| Gene Name | CG2200 |
| Organism | Drosophila melanogaster (Fruit fly) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly) |
| Enzyme Sequence | MASARNLLLLSSSRLHGHGYLEHARGQLEDLFKSANVKTVLFVPYALRDHDKYTATVRDALQPWGFNVEGLHTKPDREQALREAQAIFVGGGNTFVLLRSLYEMKLLDPIRELVLQRGLPYVGSSAGTNVATRSIHTTNDMPVAYPPSFEALALVPFNINPHYLDPEAGSRHKGETRDERLEEFVAYHGLPVLGLREGTSVRVQGEKAILLGDRNAKLFKADGGTEELAPLADLTFLLQK |
| Enzyme Length | 240 |
| Uniprot Accession Number | Q9VYH3 |
| Absorption | |
| Active Site | ACT_SITE 125; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 140; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 162; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides.; EC=3.4.13.21; |
| DNA Binding | |
| EC Number | 3.4.13.21 |
| Enzyme Function | FUNCTION: Hydrolyzes dipeptides containing N-terminal aspartate residues. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1) |
| Keywords | Cytoplasm;Dipeptidase;Hydrolase;Protease;Reference proteome;Serine protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 14605208; 20220848; 21074052; 23071443; 25294943; 25312911; 33827210; |
| Motif | |
| Gene Encoded By | |
| Mass | 26,598 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |