| IED ID | IndEnz0002018470 |
| Enzyme Type ID | protease018470 |
| Protein Name |
Dipeptidyl peptidase 4 EC 3.4.14.5 Dipeptidyl peptidase IV DPP IV DppIV |
| Gene Name | dpp4 AO090023000602 |
| Organism | Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus oryzae (Yellow koji mold) Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
| Enzyme Sequence | MKYSKLLLLLVSVVQALDVPRKPHAPTGEGSKRLTFNETVVKQAITPTSRSVQWLSGAEDGSYVYAAEDGSLTIENIVTNESRTLIPADKIPTGKEAFNYWIHPDLSSVLWASNHTKQYRHSFFADYYVQDVESLKSVPLMPDQEGDIQYAQWSPVGNTIAFVRENDLYVWDNGTVTRITDDGGPDMFHGVPDWIYEEEILGDRYALWFSPDGEYLAYLSFNETGVPTYTVQYYMDNQEIAPAYPWELKIRYPKVSQTNPTVTLSLLNIASKEVKQAPIDAFESTDLIIGEVAWLTDTHTTVAAKAFNRVQDQQKVVAVDTASNKATVISDRDGTDGWLDNLLSMKYIGPIKPSDKDAYYIDISDHSGWAHLYLFPVSGGEPIPLTKGDWEVTSILSIDQERQLVYYLSTQHHSTERHLYSVSYSTFAVTPLVDDTVAAYWSASFSANSGYYILTYGGPDVPYQELYTTNSTKPLRTITDNAKVLEQIKDYALPNITYFELPLPSGETLNVMQRLPPGFSPDKKYPILFTPYGGPGAQEVTKRWQALNFKAYVASDSELEYVTWTVDNRGTGFKGRKFRSAVTRQLGLLEAEDQIYAAQQAANIPWIDADHIGIWGWSFGGYLTSKVLEKDSGAFTLGVITAPVSDWRFYDSMYTERYMKTLSTNEEGYETSAVRKTDGFKNVEGGFLIQHGTGDDNVHFQNSAALVDLLMGDGVSPEKLHSQWFTDSDHGISYHGGGVFLYKQLARKLYQEKNRQTQVLMHQWTKKDLEE |
| Enzyme Length | 771 |
| Uniprot Accession Number | Q2UH35 |
| Absorption | |
| Active Site | ACT_SITE 618; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 695; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 730; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.; EC=3.4.14.5; |
| DNA Binding | |
| EC Number | 3.4.14.5 |
| Enzyme Function | FUNCTION: Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. {ECO:0000269|PubMed:9835566}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. is active between pH 4.0 and 9.0. {ECO:0000269|PubMed:9835566}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Frameshift (1); Glycosylation (7); Signal peptide (1) |
| Keywords | Aminopeptidase;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Serine protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9835566}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 86,875 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |