| IED ID | IndEnz0002019187 |
| Enzyme Type ID | protease019187 |
| Protein Name |
Beta-Ala-His dipeptidase EC 3.4.13.20 CNDP dipeptidase 1 Carnosine dipeptidase 1 |
| Gene Name | Cndp1 Cn1 |
| 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 | MLSPPHSGTLEKLFQYIDLHQDEFVQTLKEWVAIESDSVQPMPRLRQELFRMMALAADKLRNLGARVDSVDLGSQQMPDGQSLPTPPIILAELGNDPKKPSVCFYGHLDVQPAQKEDGWLTDPYTLTEVDGKLYGRGATDNKGPVLAWINAVSTFRALQQDLPVNVKFILEGMEEAGSVALEELVKREKDNFFSGVDYIVISDNLWLSQKKPALTCGTRGNCYFTVEVKCRDQDFHSGTFGGILNEPMADLVALLGSLVDSSGHILVPGIYDQMAPITEEEKTMYENIDLDLEEYQKSSRVERFLFDTKEELLTHLWRYPSLSIHGIEGAFDEPGTKTVIPGRVLGKFSIRLVPHMTPSVVETQVTQHLEAVFSKRNSFNKMAVSMVLGLQPWTANINGTQYLAARRAIQTVFGVDPDMIQDGSTIPIAKIFQDITQKSVMMLPLGAVDDGEHSQNEKINRWNYIQGSKLFAAFFLELSKLHSGQQVPSGAF |
| Enzyme Length | 492 |
| Uniprot Accession Number | Q66HG3 |
| Absorption | |
| Active Site | ACT_SITE 109; /evidence=ECO:0000250; ACT_SITE 174; /note=Proton acceptor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential hydrolysis of the beta-Ala-|-His dipeptide (carnosine), and also anserine, Xaa-|-His dipeptides and other dipeptides including homocarnosine.; EC=3.4.13.20; Evidence={ECO:0000250|UniProtKB:Q8BUG2, ECO:0000250|UniProtKB:Q96KN2}; CATALYTIC ACTIVITY: Reaction=carnosine + H2O = beta-alanine + L-histidine; Xref=Rhea:RHEA:59360, ChEBI:CHEBI:15377, ChEBI:CHEBI:57485, ChEBI:CHEBI:57595, ChEBI:CHEBI:57966; EC=3.4.13.20; Evidence={ECO:0000250|UniProtKB:Q8BUG2, ECO:0000250|UniProtKB:Q96KN2};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59361; Evidence={ECO:0000250|UniProtKB:Q8BUG2}; CATALYTIC ACTIVITY: Reaction=anserine + H2O = beta-alanine + N(pros)-methyl-L-histidine; Xref=Rhea:RHEA:59576, ChEBI:CHEBI:15377, ChEBI:CHEBI:57966, ChEBI:CHEBI:58445, ChEBI:CHEBI:143076; EC=3.4.13.20; Evidence={ECO:0000250|UniProtKB:Q96KN2};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59577; Evidence={ECO:0000250|UniProtKB:Q96KN2}; CATALYTIC ACTIVITY: Reaction=H2O + L-alanyl-L-histidine = L-alanine + L-histidine; Xref=Rhea:RHEA:37283, ChEBI:CHEBI:15377, ChEBI:CHEBI:57595, ChEBI:CHEBI:57972, ChEBI:CHEBI:74388; Evidence={ECO:0000250|UniProtKB:Q96KN2};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37284; Evidence={ECO:0000250|UniProtKB:Q96KN2}; CATALYTIC ACTIVITY: Reaction=glycyl-L-histidine + H2O = glycine + L-histidine; Xref=Rhea:RHEA:67376, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305, ChEBI:CHEBI:57595, ChEBI:CHEBI:169956; Evidence={ECO:0000250|UniProtKB:Q96KN2};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67377; Evidence={ECO:0000250|UniProtKB:Q96KN2}; CATALYTIC ACTIVITY: Reaction=H2O + L-homocarnosine = 4-aminobutanoate + L-histidine; Xref=Rhea:RHEA:59572, ChEBI:CHEBI:15377, ChEBI:CHEBI:57595, ChEBI:CHEBI:59888, ChEBI:CHEBI:143075; EC=3.4.13.20; Evidence={ECO:0000250|UniProtKB:Q96KN2};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59573; Evidence={ECO:0000250|UniProtKB:Q96KN2}; |
| DNA Binding | |
| EC Number | 3.4.13.20 |
| Enzyme Function | FUNCTION: Catalyzes the peptide bond hydrolysis in Xaa-His dipeptides, displaying the highest activity toward carnosine (beta-alanyl-L-histidine) and anserine (beta-alanyl-3-methyl-histidine). {ECO:0000250|UniProtKB:Q96KN2}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (6); Modified residue (1) |
| Keywords | Carboxypeptidase;Hydrolase;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;Secreted;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q96KN2}. |
| Modified Residue | MOD_RES 194; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:16641100 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 54,928 |
| Kinetics | |
| Metal Binding | METAL 107; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q96KN2; METAL 140; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q96KN2; METAL 140; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q96KN2; METAL 175; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q96KN2; METAL 203; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q96KN2; METAL 453; /note=Zinc 1; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q96KN2 |
| Rhea ID | RHEA:59360; RHEA:59361; RHEA:59576; RHEA:59577; RHEA:37283; RHEA:37284; RHEA:67376; RHEA:67377; RHEA:59572; RHEA:59573 |
| Cross Reference Brenda |