| IED ID | IndEnz0002016440 |
| Enzyme Type ID | protease016440 |
| Protein Name |
Dipeptidase 1 EC 3.4.13.19 Beta-lactamase EC 3.5.2.6 Microsomal dipeptidase Renal dipeptidase |
| Gene Name | Dpep1 Rdp |
| 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 | MLIIWWFWSLLAICASDSFRNQAENIMRTTPVIDGHNDLPWQMLTLFNNQLRKSEANLSALAETHTNIPKLRAGFVGGQFWSAYMPCDTQNKDAVKRILEQIDVIHRMCQLYPETFECVTNSSDILQAFRRGKVASLIGVEGGHLIDSSLGVLRTLYHLGMRYLTLTHNCNTPWADNWLVDKGDDEAESQGLSPFGKLVLNEMNRLGVMIDLSHVSVATMKDALQLSKAPVIFSHSSAYSVCPHRRNVPDDVLQLVKSTNSLVMVNFYNQFVSCSDSATLSQVADHLDHIKKVAGAGAVGLGGDYDGVTNLPVGLEDVSKYPDLIAELLRRNWTETEVRGLLAENLLRVFSAVELVSNIMQVPEEETIPVEKLDGSCRTFYGHSRAPSIHLQIGALLASLASLVFSLHLL |
| Enzyme Length | 410 |
| Uniprot Accession Number | P31430 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by L-penicillamine. Beta-lactamase activity is inhibited by cilastatin. {ECO:0000250|UniProtKB:P16444}. |
| Binding Site | BINDING 168; /note=Substrate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; BINDING 246; /note=Substrate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; BINDING 304; /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:P31428, 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:P31428}; CATALYTIC ACTIVITY: Reaction=2 H2O + L-cystine-bis-glycine = 2 glycine + L-cystine; Xref=Rhea:RHEA:60520, ChEBI:CHEBI:15377, ChEBI:CHEBI:35491, ChEBI:CHEBI:57305, ChEBI:CHEBI:143812; Evidence={ECO:0000250|UniProtKB:P31428}; CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000250|UniProtKB:P31428}; CATALYTIC ACTIVITY: Reaction=glycyldehydrophenylalanine + H2O = 2,3-didehydrophenylalanine + glycine; Xref=Rhea:RHEA:62704, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305, ChEBI:CHEBI:145925, ChEBI:CHEBI:145926; Evidence={ECO:0000250|UniProtKB:P31428}; |
| DNA Binding | |
| EC Number | 3.4.13.19; 3.5.2.6 |
| Enzyme Function | FUNCTION: Hydrolyzes a wide range of dipeptides including the conversion of leukotriene D4 to leukotriene E4. Hydrolyzes cystinyl-bis-glycine (cys-bis-gly) formed during glutathione degradation. Possesses also beta lactamase activity and hydrolytically inactivates beta-lactam antibiotics. {ECO:0000250|UniProtKB:P31428}.; FUNCTION: Independently of its dipeptidase activity, acts as an adhesion receptor for neutrophil recruitment from bloodstream into inflamed lungs and liver. {ECO:0000250|UniProtKB:P31428}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (3); Chain (1); Disulfide bond (3); Glycosylation (3); Lipidation (1); Metal binding (6); Propeptide (1); Sequence conflict (1); Signal peptide (1) |
| Keywords | Cell membrane;Cell projection;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: Apical cell membrane {ECO:0000250|UniProtKB:P16444}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P16444}. Cell projection, microvillus membrane {ECO:0000250|UniProtKB:P16444}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P16444}. Note=Brush border membrane. {ECO:0000250|UniProtKB:P31429}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000250|UniProtKB:P16444 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 45,522 |
| Kinetics | |
| Metal Binding | METAL 36; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 38; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 141; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 141; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 214; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 235; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073 |
| Rhea ID | RHEA:48940; RHEA:48616; RHEA:60520; RHEA:20401; RHEA:62704 |
| Cross Reference Brenda |