| IED ID | IndEnz0002019326 |
| Enzyme Type ID | protease019326 |
| Protein Name |
Asp/Glu-specific dipeptidyl-peptidase EC 3.4.14.- Dipeptidyl-peptidase 11 DPP11 |
| Gene Name | dpp11 PGN_0607 |
| Organism | Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
| Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Bacteroidia Bacteroidales Porphyromonadaceae Porphyromonas Porphyromonas gingivalis Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
| Enzyme Sequence | MKKRLLLPLFAALCLSQIAHADEGMWLMQQLGRKYAQMKERGLKMKEYDLYNPNGTSLKDAVVLFDGGCTGEVVSDRGLVLTNHHCGYDMIQAHSTLEHNYLENGFWAMREADELPNKDISVVFIDKIEDVTDYVKKELKAIKDPNSMDYLSPKYLQKLADKKAGKNFSAKNPGLSVEIKAFYGGNLYLMFTKKTYTDVRLVGAPPSSIGKFGADTDNWIWPRHTGDFSIFRIYADKNGNPAPYSEDNVPLKPKRFFNISLGGVQENDYAMIMGFPGTTHRYFTASEVDEWKSIDNDIRIRMRDIRQGVMLREMLADPQIKIMYSAKYAASQNAYKRAIGANWAIKTRGLRQNKQAMQDRLIAWGAKQGTPRYEEAVHEIDATVAKRADLRRRYWMIEEGIIRGIEFARSPIPTEDETKALQGNDASARKEAIDKIRTRYSKFANKDYSAEVDKKVAVAMLTEYLKEIPYENLPLHLRLVKDRFAGDVQAYVDDIFARSVFGSEAQFDAFAAVPSVEKLAEDPMVLFASSVFDEYRKLYNELRPYDDPILRAQRTYIAGLLEMDGDQDQFPDANLTLRFTYGQVKGYSPRDNVYYGHQTTLDGVMEKEDPDNWEFVVDPKLKAVYERKDFGRYADRSGRMPVAFCATTHTTGGNSGSPVMNANGELIGLNFDRNWEGVGGDIQYLADYQRSIIVDIRYVLLVIDKVGGCQRLLDEMNIVP |
| Enzyme Length | 720 |
| Uniprot Accession Number | B2RID1 |
| Absorption | |
| Active Site | ACT_SITE 85; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:V5YM14, ECO:0000305|PubMed:26057589"; ACT_SITE 227; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:V5YM14, ECO:0000305|PubMed:26057589"; ACT_SITE 655; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:V5YM14, ECO:0000305|PubMed:21896480, ECO:0000305|PubMed:26057589" |
| Activity Regulation | ACTIVITY REGULATION: Enzyme activity is completely blocked by diisopropyl-fluorophosphates, moderately by phenylmethylsulfonyl fluoride (PMSF) and 4-(2-methyl)benzenesulfonyl fluoride, and slightly by pepstatin in vitro. {ECO:0000269|PubMed:21896480}. |
| 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 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. Is involved in amino acid metabolism and bacterial growth of asaccharolytic P.gingivalis, that utilizes amino acids from extracellular proteinaceous nutrients as energy and carbon sources. {ECO:0000269|PubMed:21896480, ECO:0000269|PubMed:23246913}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:21896480}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (24); Chain (1); Disulfide bond (1); Helix (38); Mutagenesis (5); Signal peptide (1); Site (1); Turn (4) |
| Keywords | 3D-structure;Aminopeptidase;Disulfide bond;Hydrolase;Protease;Serine protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:21896480}. Note=Is exclusively cell-associated. {ECO:0000269|PubMed:21896480}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (7) |
| Cross Reference PDB | 4XZY; 4Y01; 4Y02; 4Y04; 5JWF; 6JTB; 6JTC; |
| Mapped Pubmed ID | 28588213; 31537874; |
| Motif | |
| Gene Encoded By | |
| Mass | 81,938 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |