| IED ID | IndEnz0002019018 |
| Enzyme Type ID | protease019018 |
| Protein Name |
Asp/Glu-specific dipeptidyl-peptidase EC 3.4.14.- Dipeptidyl-peptidase 11 DPP11 |
| Gene Name | dpp11 CAPGI0001_1068 |
| Organism | Capnocytophaga gingivalis |
| Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Flavobacteriia Flavobacteriales Flavobacteriaceae Capnocytophaga Capnocytophaga gingivalis Capnocytophaga gingivalis |
| Enzyme Sequence | MKRFFKMALFLGVSALYGQQGGMWIPSLLEGMNAKEMKTLGMKMTVADIYSVNKSSLKDAAPHFNGGCSSEVISDKGLLLTNHHCGYGQIQAHSTLQNDYLANGFWAKSLAEELPNKNLKVTFMVRIDDVTKQVLKGTESITDETEKAKLIEKNIAEVIKTAPKEAWQENSVKAFYDGNQYILFVTETFKDVRLVGAPPSSIGKFGSDTDNWVWPRHTGDFSLFRIYADKNNRPAEYSKDNVPYKPKHFFPISLKGVKEGDFVLVFGYPGTTQEYLPSAAVAQIENVINPARIGIRDIVLKVQDSYMRKDQGIKIKYAAKYARVANYWKKWMGETKGLKKSGAVALKQQQEAKFQQAIQKANKQAQYGNLLSDFNRLYKEIEPYTLAANLNSEFIFRNIDLLSNGSRLLQLEKALEDKGEQSFNDRKKNLLNTFKEIFKDNDKQVDKDVFEKVVVFYAANMPKNLLINSLKNFDAKKLADNLYNNSFLTSLSGVESVLNLSAAEFKERMKNDVGIQFVRELKEMNDTQVFPVYDRLNTQIHALQRTYMKAILEFSKPSDRIFPDANGTLRVTYGKVAGFSPADAVTYSAHTTLDGVMEKYVPGDYEFDVPQHLRDLQAKKDFGRYGDKNGKMPLCFLSTCHTTGGNSGSPAIDANGNLIGLNFDRVWEGTMSDIHYDPKLCRNIMVDIRYVLFVIDKYAGAGHLVNEMKLIK |
| Enzyme Length | 712 |
| Uniprot Accession Number | C2M741 |
| Absorption | |
| Active Site | ACT_SITE 84; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:V5YM14; ACT_SITE 220; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:V5YM14; ACT_SITE 647; /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. Shows a strict specificity for acidic residues (Asp or Glu) in the P1 position, and has probably a hydrophobic residue preference at the P2 position. Preferentially cleaves the synthetic substrate Leu-Asp-methylcoumaryl-7-amide (Leu-Asp-MCA) as compared to Leu-Glu-MCA. {ECO:0000269|PubMed:23246913}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Signal peptide (1); Site (1) |
| Keywords | Aminopeptidase;Hydrolase;Protease;Serine protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| 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 | 80,432 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |