| IED ID | IndEnz0002005220 |
| Enzyme Type ID | protease005220 |
| Protein Name |
Dipeptidyl peptidase 3 EC 3.4.14.4 Dipeptidyl aminopeptidase III Dipeptidyl arylamidase III Dipeptidyl peptidase III DPP III Enkephalinase B |
| Gene Name | Dpp3 |
| Organism | Rattus norvegicus (Rat) |
| 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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MADTQYILPNDIGVSSLDCREAFRLLSPTERLYAHHLSRAAWYGGLAVLLQTSPEAPYIYALLSRLFRAQDPDQLRQHALAEGLTEEEYQAFLVYAAGVYSNMGNYKSFGDTKFVPNLPKEKLERVILGSKAAQQHPEEVRSLWQTCGELMFSLEPRLRHLGLGKEGVTTYFSGDCAMEDAKLAQDFLDSQNLSAYNTRLFKVVGQEGKYHYEVRLASVLNTEPALDSELTSKLKSYEFQGNHFQVTRGDYAPILQKVVEHLEKAKAYAANSHQEQMLAQYVESFTQGSIEAHKRGSRFWIQDKGPIVESYIGFIESYRDPFGSRGEFEGFVAMVNKDMSAKFERLVASAEQLLKELPWPPAFEKDKFLTPDFTSLDVLTFAGSGIPAGINIPNYDDLRQTEGFKNVSLGNVLAVAYATKREKLTFMEEEDKDLYIRWKGPSFDVQVGLHELLGHGSGKLFVQDEKGAFNFDQETVINPETGEQIQSWYRSGETWDSKFSTIASSYEECRAESVGLYLCLNPQVLQIFGFEGTDAEDVIYVNWLNMVRAGLLALEFYTPETANWRQAHMQARFVILRVLLEAGEGLVTVTPTTGSDGRPDARVHLDRSKIRSVGKPALERFLRRLQVLKSTGDVVAGRALYEGYAAVTDAPPECFLTLRDTVLLRKESRKLIVQPNTRLEGSEVQLVEYEASAAGLIRSFCERFPEDGPELEEVLTQLATADAQFWRDQVQEAPSGQA |
| Enzyme Length | 738 |
| Uniprot Accession Number | O55096 |
| Absorption | |
| Active Site | ACT_SITE 451; /evidence=ECO:0000269|PubMed:10387075 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by spinorphin, an opioid peptide derived from hemoglobin. {ECO:0000250}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.; EC=3.4.14.4; |
| DNA Binding | |
| EC Number | 3.4.14.4 |
| Enzyme Function | FUNCTION: Cleaves and degrades bioactive peptides, including angiotensin, Leu-enkephalin and Met-enkephalin (By similarity). Also cleaves Arg-Arg-beta-naphthylamide. {ECO:0000250|UniProtKB:Q9NY33}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Initiator methionine (1); Metal binding (3); Modified residue (1); Mutagenesis (5) |
| Keywords | Acetylation;Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000250|UniProtKB:Q9NY33 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 83,039 |
| Kinetics | |
| Metal Binding | METAL 450; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:10387075; METAL 455; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:10387075; METAL 508; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9NY33 |
| Rhea ID | |
| Cross Reference Brenda |