Detail Information for IndEnz0002019326
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