| IED ID | IndEnz0002016282 |
| Enzyme Type ID | protease016282 |
| Protein Name |
Probable dipeptidyl peptidase 4 EC 3.4.14.5 Dipeptidyl peptidase IV DPP IV DppIV |
| Gene Name | dpp4 AFUB_066450 |
| Organism | Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus) |
| Enzyme Sequence | MKWSILLLVGCAAAIDVPRQPYAPTGSGKKRLTFNETVVKRAISPSAISVEWISTSEDGDYVYQDQDGSLKIQSIVTNHTQTLVPADKVPEDAYSYWIHPNLSSVLWATNYTKQYRYSYFADYFIQDVQSMKLRPLAPDQSGDIQYAQWSPTGDAIAFVRDNNVFVWTNASTSQITNDGGPDLFNGVPDWIYEEEILGDRFALWFSPDGAYLAFLRFNETGVPTFTVPYYMDNEEIAPPYPRELELRYPKVSQTNPTVELNLLELRTGERTPVPIDAFDAKELIIGEVAWLTGKHDVVAVKAFNRVQDRQKVVAVDVASLRSKTISERDGTDGWLDNLLSMAYIGPIGESKEEYYIDISDQSGWAHLWLFPVAGGEPIALTKGEWEVTNILSIDKPRQLVYFLSTKHHSTERHLYSVSWKTKEITPLVDDTVPAVWSASFSSQGGYYILSYRGPDVPYQDLYAINSTAPLRTITSNAAVLNALKEYTLPNITYFELALPSGETLNVMQRLPVKFSPKKKYPVLFTPYGGPGAQEVSKAWQALDFKAYIASDPELEYITWTVDNRGTGYKGRAFRCQVASRLGELEAADQVFAAQQAAKLPYVDAQHIAIWGWSYGGYLTGKVIETDSGAFSLGVQTAPVSDWRFYDSMYTERYMKTLESNAAGYNASAIRKVAGYKNVRGGVLIQHGTGDDNVHFQNAAALVDTLVGAGVTPEKLQVQWFTDSDHGIRYHGGNVFLYRQLSKRLYEEKKRKEKGEAHQWSKKSVL |
| Enzyme Length | 765 |
| Uniprot Accession Number | B0Y6C5 |
| Absorption | |
| Active Site | ACT_SITE 613; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 690; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 725; /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. Contributes to pathogenicity. {ECO:0000269|PubMed:9234752}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.7 to 7.0. {ECO:0000269|PubMed:9234752}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Glycosylation (9); Sequence conflict (3); Signal peptide (1) |
| Keywords | Aminopeptidase;Glycoprotein;Hydrolase;Protease;Secreted;Serine protease;Signal;Virulence |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9234752}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..14; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 85,876 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.38 mM for Gly-Pro pNA and Ala-Pro pNA {ECO:0000269|PubMed:9234752}; KM=0.15 mM for Arg-Pro pNA {ECO:0000269|PubMed:9234752}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |