| IED ID | IndEnz0002003012 |
| Enzyme Type ID | protease003012 |
| Protein Name |
Probable dipeptidyl peptidase 4 EC 3.4.14.5 Dipeptidyl peptidase IV DPP IV DppIV |
| Gene Name | dpp4 AN6438 |
| Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Enzyme Sequence | MKLSVLSVLLVSVAQAAAAPWRPREPRAAGSKRLTFNETVISAALSPSSISVQWIATENDGDYVYQEEDGSIKIESIVTNRSQTIVPAEKIPADAYSYWISPDLSAVLWATNYTKQYRHSFFADYYIQDVETLETVPLVEDMVGDIQYAEWSPSGDSIAFVRGNNLWTWSDGTVTAITKDGGPDMFHGVPDWIYEEEILGDRFALWFSPDSELLAFLTFNETGVPTFTVQYFMDNQEIAPPYPRELDIRYPKVSETNPTVKLNILQLSDNTVSTIPIDVFDPSELIVGEVAWVTDTHTELAVKAFNRVQDESKVVIVETASGETKIAHERDGTDGWLDNLLSISYVGPLALGSGDASSAYYVDLSDHSGWTHLYLFSTSGGDPIPLTEGEWEVTSIVSIDQERELVYYLSTQHHSTERHLYSVSYRTFEITPLVDDTVEAYWSVSFSAKAGYYILTYAGPSVPYQELYSVNQTAPLRTLTSNAALIEKLEEYALPNISYFELEIPSGEKLNVMQRLPVGFSPDKKYPVLFTPYGGPGAQEVSKRWQSLDFNAYIASDPELEYVTWTVDNRGTGYRGREFRSLVAKQLGKLEAEDQVYAAKQAAKLDWVDSEHIAIWGWSYGGYLTGKVLETDSGAFSLGLLTAPVSDWRLYDSMYTERYMKTLSTNAEGYNTTAIRHTDGFKNVEGGFLIQHGTGDDNVHFQNAAALGDTLIGNGVTPEKMQVQWFTDSDHSIRYNGGNVFLYRQLAQRLYKEKNRAKKEQHQWSKRSQDWVV |
| Enzyme Length | 773 |
| Uniprot Accession Number | Q5AZ42 |
| Absorption | |
| Active Site | ACT_SITE 619; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 696; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 731; /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:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (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:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 86,855 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |