| IED ID | IndEnz0002019330 |
| Enzyme Type ID | protease019330 |
| Protein Name |
Dipeptidyl-peptidase 5 DPP5 EC 3.4.14.- MER236725 |
| Gene Name | dpp5 POREN0001_0643 |
| 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 | MKRTILSLLAAVSLAIPVYAAGYSDGNPTQQTSQSSMMTPEMLLTMARIGGFSLSPNGKQVVYSVSLPSIQDNKAKTQLFFVNSDGSGRKALTDGTRTAVSPRWIEDGKRIAYLTVIEGEMQLVSILPDGTDQRQVTRIPGGITGYLYSQDGKQLVYTADIKLPNEAKDRNPDLDKISGRVITDLMYKHWDEWVETAPHTFVASLAQQPITQGKDLLEGELFEAPMKPHSDESDIAITPDGKGIAYASRKKTGLEYSISTNSDIYYYDLTTGTTTNLTEGMMGYDTHPSFSPDGKYMTWCSMERDGYESDLIRLFLLDRTTGEKTYLTEGFEYNVEQPTWSQDGKSIYFIACVEAESHLYELTLKNKKIRRITQGQMDYVGFDLQGTTLVAARQSMLAPTDLYRIDLKKGTATAITKENESTLAQLGDIRCEKRWMNTTNGEKMLVWVLYPANFDASKKYPSILYCQGGPQSTISQFWSYRWNPRIMAENGYIVILPNRHGVPGFGKAWNEQISGDYGGQNMRDYLTAADEMKKESYIDPNGMGCVGASYGGFSVYWLAGHHEKRFNCFIAHAGIFNLEAQYLETEEKWFANWDMGGAPWEKSNATAQRTFATSPHLFVDKWDTPILIIHGERDYRILASQGMMAFDAARMHGVPTEMLLYPDENHWVLQPQNAVLWQRTFFRWLDRWLKK |
| Enzyme Length | 691 |
| Uniprot Accession Number | C3J8X2 |
| Absorption | |
| Active Site | ACT_SITE 549; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:B2RIT0; ACT_SITE 634; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:B2RIT0; ACT_SITE 666; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:B2RIT0 |
| 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. Prefers Ala and hydrophobic residues at the P1 position, and has no preference for P2 residues. Shows the highest dipeptidyl peptidase activity toward the synthetic substrate Lys-Ala-methylcoumaryl-7-amide (Lys-Ala-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 | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.7, using Lys-Ala-MCA as substrate. {ECO:0000269|PubMed:25494328}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Signal peptide (1) |
| Keywords | Aminopeptidase;Hydrolase;Periplasm;Protease;Reference proteome;Serine protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:B2RIT0}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 78,098 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=110 uM for Lys-Ala-MCA (at 37 degrees Celsius and pH 7.0) {ECO:0000269|PubMed:25494328}; KM=196 uM for Met-Leu-MCA (at 37 degrees Celsius and pH 7.0) {ECO:0000269|PubMed:25494328}; KM=257 uM for Ser-Tyr-MCA (at 37 degrees Celsius and pH 7.0) {ECO:0000269|PubMed:25494328}; KM=993 uM for Gly-Phe-MCA (at 37 degrees Celsius and pH 7.0) {ECO:0000269|PubMed:25494328}; Note=kcat is 21213 sec(-1) with Lys-Ala-MCA as substrate. kcat is 5175 sec(-1) with Met-Leu-MCA as substrate. kcat is 3468 sec(-1) with Ser-Tyr-MCA as substrate. kcat is 10378 sec(-1) with Gly-Phe-MCA as substrate. {ECO:0000269|PubMed:25494328}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |