| IED ID | IndEnz0002003178 |
| Enzyme Type ID | protease003178 |
| Protein Name |
Dipeptidyl-peptidase 7 DPP7 EC 3.4.14.- MER278904 |
| Gene Name | dpp7 POREN0001_0291 |
| Organism | Porphyromonas endodontalis (strain ATCC 35406 / BCRC 14492 / JCM 8526 / NCTC 13058 / HG 370) |
| Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Bacteroidia Bacteroidales Porphyromonadaceae Porphyromonas Porphyromonas endodontalis Porphyromonas endodontalis (strain ATCC 35406 / BCRC 14492 / JCM 8526 / NCTC 13058 / HG 370) |
| Enzyme Sequence | MKLKRILLSVALLCGIGTTAMADKGMWLLNELNQQNYERMKELGFKLSPEQLYSLGQPSVASAVVIFGGGCTGITVSNEGLIFTNHHCGFGAIQSQSTVDHDYLRDGFRSNNHVEELPIPGLSVRYLREIVDVTPRIEAAVKGAKSEMERMQIIEELSQKINAEYTKGSTVVGEVTPYYAGNKYYVVVYNVFQDVRLVMAPPSSVGKFGGDTDNWMWTRHTGDFSVFRVYADANNNPALYSQNNKPYKPISYAPVSLNGYREGDYAMTIGFPGSTNRYLTSWGVEDVVNNENSPRIEVRGIKQAIWKEAMEADQATRIKYASKYAQSSNYWKNSIGMNRGLKNLDVVNRKRAEEKAFEAWIAKNNSQSTYGHILPGLKADYAKSAAISKDINYLYETLWGGTEIVRLARDVNSVGRIQAADMPKYKGRLEELYKDYLPSLDVKVLPAMLDIVRQRVSADCQPDIFKFIDKKFKGSTEKYAQYVFEKSIVPYADKVKDFLNLPADKQKKILDKDPAVALFNSVLPAIMQAQDKSEEMMLNIEKGKREYFAASRIMDPNRQMPSDANFTMRMSYGSIKGYAPKDGAWYNYYTTEQGVFEKQDPTSSEFAVQPEILSLLRSKDFGQYGVGDHLRLCFLSDNDITGGNSGSPVFNGNGELIGLAFDGNWEAMSGDIEFEPDLQRTISVDIRYVLFMIDKWAKMPHLIKELNLVKGDQRDLMPAGKGGNCSHKKAQTCAKKECSKGKKCAEKSATCISAMKDGKPCKTEKACAAGQKSAEKKANCCSTMKDGKPCTGDKDCAKSGKACCGKNKEAAAKKASKK |
| Enzyme Length | 818 |
| Uniprot Accession Number | C3JAQ3 |
| Absorption | |
| Active Site | ACT_SITE 87; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:V5YM14; ACT_SITE 223; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:V5YM14; ACT_SITE 645; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:V5YM14 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.14.- |
| Enzyme Function | FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Most efficiently cleaves the synthetic substrate Met-Leu-methylcoumaryl-7-amide (Met-Leu-MCA), and slowly hydrolyzes Leu-Gln-, Lys-Ala-, Leu-Arg, and Ala-Asn-MCA. Is likely involved in amino acid metabolism and bacterial growth/survival of asaccharolytic P.endodontalis, that utilizes amino acids from extracellular proteinaceous nutrients as energy and carbon sources. {ECO:0000269|PubMed:25494328}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Signal peptide (1); Site (1) |
| Keywords | Aminopeptidase;Hydrolase;Protease;Reference proteome;Serine protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 91,085 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |