| IED ID | IndEnz0002018689 |
| Enzyme Type ID | protease018689 |
| Protein Name |
Dipeptidase 2 EC 3.4.13.19 Membrane-bound dipeptidase 2 MBD-2 |
| Gene Name | Dpep2 Mbd2 |
| Organism | Mus musculus (Mouse) |
| 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 Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MSLTGLKGHWVLGHGLSVFLLVLLLLGPSQPLIWTQTKPGFSGASTTSSIPRALTKPDISSIPTTPGNPNFPDLRDRARALMQEFPLIDGHNDMPLVLRQFYQNGLQDANLRNFTHGQTSLDRLKDGLVGAQFWSAYVPCQTQDRDALRLTLEQIDLIRRICASYSELELVTSVKALNSTQKLACLIGVEGGHSLDNSLAVLRSFYLLGVRYLTLTHTCNTPWAETSSKGVHAFYSSVTGLTSFGEKVVAEMNRLGMMVDLSHVSDAAARRALEVSQAPVIFSHSAARAVCPNARNLPDDLLQLLKKNGGIVMVTFSVGVLPCNPLANVSTVADHFDHIRSVIGSEFIGIGGDYDGTKQFPQGLEDVSTYPVLIEELLRRGWNEQELQGILRGNLLRVFRQVEQVRDKSKWQSPLEDMIPEEQLDSACHSALRPQKQHPEKNQPETPEYHILKFSHSKSSPHIVPSLAIVATLLGLIV |
| Enzyme Length | 478 |
| Uniprot Accession Number | Q8C255 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by L-penicillamine. {ECO:0000269|PubMed:12738806}. |
| Binding Site | BINDING 217; /note=Substrate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; BINDING 295; /note=Substrate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; BINDING 353; /note=Substrate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid; Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869, ChEBI:CHEBI:77460; EC=3.4.13.19; Evidence={ECO:0000255|PROSITE-ProRule:PRU10073, ECO:0000269|PubMed:12738806}; CATALYTIC ACTIVITY: Reaction=H2O + leukotriene D4 = glycine + leukotriene E4; Xref=Rhea:RHEA:48616, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305, ChEBI:CHEBI:57462, ChEBI:CHEBI:63166; Evidence={ECO:0000269|PubMed:12738806};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48617; Evidence={ECO:0000305|PubMed:12738806}; |
| DNA Binding | |
| EC Number | 3.4.13.19 |
| Enzyme Function | FUNCTION: Dipeptidase that hydrolyzes leukotriene D4 (LTD4) into leukotriene E4 (LTE4) (PubMed:12738806). Does not hydrolyze cystinyl-bis-glycine (PubMed:12738806). {ECO:0000269|PubMed:12738806}.; FUNCTION: Independently of its dipeptidase activity can also modulate macrophage inflammatory response by acting as a regulator of NF-kappa-B inflammatory signaling pathway. {ECO:0000269|PubMed:30899700}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (4); Binding site (3); Chain (1); Compositional bias (1); Disulfide bond (3); Glycosylation (2); Lipidation (1); Metal binding (6); Propeptide (1); Region (1); Sequence conflict (3); Signal peptide (1) |
| Keywords | Alternative splicing;Dipeptidase;Disulfide bond;GPI-anchor;Glycoprotein;Hydrolase;Lipid metabolism;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Zinc |
| Interact With | |
| Induction | INDUCTION: Up-regulated during CVB3-induced viral myocarditis in the cardiac infiltrating macrophages. {ECO:0000269|PubMed:30899700}. |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12738806}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12738806}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12466851; 20562862; 21677750; |
| Motif | |
| Gene Encoded By | |
| Mass | 52,664 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5 uM for LTD4 {ECO:0000269|PubMed:12738806}; |
| Metal Binding | METAL 91; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 93; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 190; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 190; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 263; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 284; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073 |
| Rhea ID | RHEA:48940; RHEA:48616; RHEA:48617 |
| Cross Reference Brenda |