| IED ID | IndEnz0002019012 |
| Enzyme Type ID | protease019012 |
| Protein Name |
Dipeptidase 2 EC 3.4.13.19 |
| Gene Name | Dpep2 |
| 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 | MSLKGLEGHWVLSQVFLLVVVLLLLGPSEPLIRAQTKPGIADASTAPSPLRTLTKPAIFSIPTTPGNPNFPDLRDRTRALMQDFPLIDGHNDLPLVLRQFYQNGLQDTNLRNFTHGQTSLNRLKDGFVGAQFWSAYVPCQTQDRDALRLTLEQIDLIRRMCASYSELELVTSVQALNSTQKLACLIGVEGGHSLDNSLAVLRSFYLLGVRYLTLTHTCNTPWAESSSKDVHSFYSSVKGLTSFGEKVVAEMNRLGMMIDLSHVSDATARQALEVSQAPVIFSHSAARAVCPNARNLPDDILQLLKKNGGIVMVTFAVGVLPCNPLANVSTVADHFDHIRTVIGSEFIGVGGDYDGTKQFPQGLEDVSTYPVLIEELLRRGWGEQELQGVLRGNLLRVFRQVEQVREKNKWQSPLEDMIPEEQLDSACHSVLPHRRQYPEKDPPETPDSHTHKLSPKMPYSKSSPLRASSLTIMATFLGLLI |
| Enzyme Length | 481 |
| Uniprot Accession Number | Q5M872 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by L-penicillamine. {ECO:0000250|UniProtKB:Q8C255}. |
| Binding Site | BINDING 216; /note=Substrate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; BINDING 294; /note=Substrate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; BINDING 352; /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:0000250|UniProtKB:Q8C255, ECO:0000255|PROSITE-ProRule:PRU10073}; 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:0000250|UniProtKB:Q8C255};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48617; Evidence={ECO:0000250|UniProtKB:Q8C255}; |
| DNA Binding | |
| EC Number | 3.4.13.19 |
| Enzyme Function | FUNCTION: Dipeptidase that hydrolyzes leukotriene D4 (LTD4) into leukotriene E4 (LTE4). Does not hydrolyze cystinyl-bis-glycine. {ECO:0000250|UniProtKB:Q8C255}.; 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:0000250|UniProtKB:Q8C255}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (3); Chain (1); Compositional bias (1); Disulfide bond (3); Glycosylation (2); Lipidation (1); Metal binding (6); Propeptide (1); Region (1); Signal peptide (1) |
| Keywords | Dipeptidase;Disulfide bond;GPI-anchor;Glycoprotein;Hydrolase;Lipid metabolism;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8C255}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q8C255}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 53,285 |
| Kinetics | |
| Metal Binding | METAL 90; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 92; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 189; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 189; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 262; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 283; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073 |
| Rhea ID | RHEA:48940; RHEA:48616; RHEA:48617 |
| Cross Reference Brenda |