| IED ID | IndEnz0002008175 |
| Enzyme Type ID | protease008175 |
| Protein Name |
Xaa-Arg dipeptidase EC 3.4.13.4 |
| Gene Name | Pm20d2 Acy1l2 Gm424 |
| 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 | MGPVVERPAEPGTSSAAELELLKRRAAERIDEAAERLGALSRAIWSAPELAYEEHRAHGELTRFFECEPPAASWAVQPHFGLPTAFRAEWAPPESAAGPRALQVAFLCEYDALPALGHACGHNLIAEVGVAAALGLRAALESIAAPPPVKVIVLGTPAEEDGGGKIDLIEAGAFENLDVVFMAHPSQENAAYLPDVAEHDVTVKYYGKASHAAAYPWEGVNALDAAVLAYTNLSVLRQQMKPTWRVHGIIKNGGVKPNIIPSYSELVYYFRAPSMKELQVLTKKAEDCFRAAALATGCTVDIESEAHDYYNVIPNKTLCSAYTENGKKLGMEFISEDAVLNGPSGSTDFGNVSFVVPGIHPYFYIGTDALNHTEQYTEAAGSQAAQLYTLRTAKALAMTALDVIFKPALLEGVRKEFKCKLQEEQLLNTAA |
| Enzyme Length | 431 |
| Uniprot Accession Number | A3KG59 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=beta-alanyl-L-lysine + H2O = beta-alanine + L-lysine; Xref=Rhea:RHEA:59608, ChEBI:CHEBI:15377, ChEBI:CHEBI:32551, ChEBI:CHEBI:57966, ChEBI:CHEBI:143161; EC=3.4.13.4; Evidence={ECO:0000269|PubMed:24891507};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59609; Evidence={ECO:0000305|PubMed:24891507}; CATALYTIC ACTIVITY: Reaction=beta-alanyl-L-arginine + H2O = beta-alanine + L-arginine; Xref=Rhea:RHEA:59616, ChEBI:CHEBI:15377, ChEBI:CHEBI:32682, ChEBI:CHEBI:57966, ChEBI:CHEBI:143157; EC=3.4.13.4; Evidence={ECO:0000269|PubMed:24891507};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59617; Evidence={ECO:0000305|PubMed:24891507}; CATALYTIC ACTIVITY: Reaction=beta-alanyl-L-ornithine + H2O = beta-alanine + L-ornithine; Xref=Rhea:RHEA:59612, ChEBI:CHEBI:15377, ChEBI:CHEBI:46911, ChEBI:CHEBI:57966, ChEBI:CHEBI:143162; EC=3.4.13.4; Evidence={ECO:0000269|PubMed:24891507};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59613; Evidence={ECO:0000305|PubMed:24891507}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(4-aminobutanoyl)-L-lysine = 4-aminobutanoate + L-lysine; Xref=Rhea:RHEA:59620, ChEBI:CHEBI:15377, ChEBI:CHEBI:32551, ChEBI:CHEBI:59888, ChEBI:CHEBI:143159; EC=3.4.13.4; Evidence={ECO:0000269|PubMed:24891507};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59621; Evidence={ECO:0000305|PubMed:24891507}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(4-aminobutanoyl)-L-arginine = 4-aminobutanoate + L-arginine; Xref=Rhea:RHEA:59628, ChEBI:CHEBI:15377, ChEBI:CHEBI:32682, ChEBI:CHEBI:59888, ChEBI:CHEBI:143158; EC=3.4.13.4; Evidence={ECO:0000269|PubMed:24891507};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59629; Evidence={ECO:0000305|PubMed:24891507}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(4-aminobutanoyl)-L-ornithine = 4-aminobutanoate + L-ornithine; Xref=Rhea:RHEA:59624, ChEBI:CHEBI:15377, ChEBI:CHEBI:46911, ChEBI:CHEBI:59888, ChEBI:CHEBI:143160; EC=3.4.13.4; Evidence={ECO:0000269|PubMed:24891507};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59625; Evidence={ECO:0000305|PubMed:24891507}; |
| DNA Binding | |
| EC Number | 3.4.13.4 |
| Enzyme Function | FUNCTION: Catalyzes the peptide bond hydrolysis in dipeptides having basic amino acids lysine, ornithine or arginine at C-terminus. Postulated to function in a metabolite repair mechanism by eliminating alternate dipeptide by-products formed during carnosine synthesis. {ECO:0000269|PubMed:24891507}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Chain (1); Sequence conflict (1) |
| Keywords | Alternative splicing;Carboxypeptidase;Hydrolase;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 14610273; 16602821; 21677750; |
| Motif | |
| Gene Encoded By | |
| Mass | 46,482 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 mM for beta-alanyl-L-lysine {ECO:0000269|PubMed:24891507}; KM=1.9 mM for beta-alanyl-L-ornithine {ECO:0000269|PubMed:24891507}; KM=6.8 mM for beta-alanyl-L-arginine {ECO:0000269|PubMed:24891507}; KM=2.6 mM for N(2)-(4-aminobutanoyl)-L-lysine {ECO:0000269|PubMed:24891507}; KM=1.35 mM for N(2)-(4-aminobutanoyl)-L-ornithine {ECO:0000269|PubMed:24891507}; Vmax=17.4 umol/min/mg enzyme toward beta-alanyl-L-lysine {ECO:0000269|PubMed:24891507}; Vmax=30.7 umol/min/mg enzyme toward beta-alanyl-L-ornithine {ECO:0000269|PubMed:24891507}; Vmax=27 umol/min/mg enzyme toward N(2)-(4-aminobutanoyl)-L-lysine {ECO:0000269|PubMed:24891507}; Vmax=12.5 umol/min/mg enzyme toward N(2)-(4-aminobutanoyl)-L-ornithine {ECO:0000269|PubMed:24891507}; |
| Metal Binding | |
| Rhea ID | RHEA:59608; RHEA:59609; RHEA:59616; RHEA:59617; RHEA:59612; RHEA:59613; RHEA:59620; RHEA:59621; RHEA:59628; RHEA:59629; RHEA:59624; RHEA:59625 |
| Cross Reference Brenda |