| IED ID | IndEnz0002006795 |
| Enzyme Type ID | protease006795 |
| Protein Name |
Asp/Glu-specific dipeptidyl-peptidase EC 3.4.14.- Dipeptidyl-peptidase 11 DPP11 |
| Gene Name | dpp11 PeDPP11 |
| 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 | MNKRFFPTLLLAFVCSTLAYADGGMWLMQQINGQVARMKSLGMQLEAADIYNPNGSSLKDAVVMFDGGCTGVLVSNQGLLLTNHHCGYDQIQKHSSVQHNYLKDGFWSYSLAEELVNPGLEVEIVDEITDVTAAVKKELERIKKPSGLEFLSPRYLSSLAPEIVGKKAASRPGYRYEIKAFYGGNRYYMFTKKVFRDVRLVAAPPSSIGKFGSDTDNWAWPRHTGDFSIFRLYADKNGNPAEYSKDNVPYRPKRWVKVNAQGVKEGDFALIMGYPGTTYKFFTADEVTEWSEIDNNIRIEMRGILQDVMLREMLADPKINIMYAAKYASSQNGYKRAQGANWAIRRRSLREIKLAQQQEVLAWAKQKGIATTEEAVRAISKAIEGRQDLRMRQRYLLEGILMGIEMSNAPAADSDIADHWDDPARREAGLQSIRKQFEAFFNKDYSPEVEKDQLAIALLTRYAERIPAEKQPISIREGIAEYGSAKAYVEMIFDKSIYASRERFEEFMKNPDRDRLLRDPMSRFAASVAYEHQKLAKEVAAFDAPLAAAQRSYVASVLDMKGQPNLAPDANLTLRFTYGEIKGYQPRDVVTYGAKSTLEGVMEKEDPNNWEYVVDPKLKALYEAKNYGRYANSDGSMPVNFCATTHTTGGNSGSPVMNARGELIGLNFDRNWEGVGGDIEYLPNYQRSIILDIRYLLFIIDKFAGCQRLIDEIQPQF |
| Enzyme Length | 717 |
| Uniprot Accession Number | F8WQK8 |
| Absorption | |
| Active Site | ACT_SITE 85; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:V5YM14"; ACT_SITE 226; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:V5YM14"; ACT_SITE 652; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:V5YM14, ECO:0000305|PubMed:21896480" |
| 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. 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:21896480}. |
| 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 (22); Chain (1); Helix (38); Mutagenesis (2); Signal peptide (1); Site (1); Turn (7) |
| Keywords | 3D-structure;Aminopeptidase;Direct protein sequencing;Hydrolase;Protease;Secreted;Serine protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21896480}. Cell surface {ECO:0000269|PubMed:21896480}. Note=Is observed in both cell-associated and soluble extracellular forms. {ECO:0000269|PubMed:21896480}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000269|PubMed:21896480 |
| Structure 3D | X-ray crystallography (5) |
| Cross Reference PDB | 5JWG; 5JWI; 5JXK; 5JXP; 5JY0; |
| Mapped Pubmed ID | 28588213; |
| Motif | |
| Gene Encoded By | |
| Mass | 81,096 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |