| IED ID | IndEnz0002005830 |
| Enzyme Type ID | protease005830 |
| Protein Name |
Dipeptidyl-peptidase 5 DPP5 EC 3.4.14.- MER034615 |
| Gene Name | dpp5 PGN_0756 |
| 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 | MNKKIFSMMAASIIGSAAMTPSAGTNTGEHLTPELFMTLSRVSEMALSPDGKTAVYAVSFPDVKTNKATRELFTVNLDGSGRKQITDTESNEYAPAWMADGKRIAFMSNEGGSMQLWVMNADGTERRQLSNIEGGITGFLFSPDEKQVLFTKDIKFGKRTKDIYPDLDKATGRIITDLMYKHWDEWVETIPHPFIANATDGMITTGKDIMEGEPYEAPMKPWSGIEDFSWSPDGQNIAYASRKKTGMAYSLSTNSDIYIYNLTSGRTHNISEGMMGYDTYPKFSPDGKSIAWISMERDGYESDLKRLFVADLATGKRTHVNPTFDYNVDMIQWAPDSKGIYFLACKEAETNLWEITLKTGKIRQITQGQHDYADFSVRNDVMLAKRHSFELPDDLYRVNPKNGAAQAVTAENKAILDRLTPIACEKRWMKTTDGGNMLTWVVLPPDFDKNKKYPAILYCQGGPQNTVSQFWSFRWNLRLMAEQGYIVIAPNRHGVPGFGQKWNEQISGDYGGQNMRDYLTAVDEMKKEPYVDGDRIGAVGASYGGFSVYWLAGHHDKRFAAFIAHAGIFNLEMQYATTEEMWFANWDIGGPFWEKDNVVAQRTYATSPHKYVQNWDTPILMIHGELDFRILASQAMAAFDAAQLRGVPSEMLIYPDENHWVLQPQNALLFHRTFFGWLDRWLKK |
| Enzyme Length | 684 |
| Uniprot Accession Number | B2RIT0 |
| Absorption | |
| Active Site | ACT_SITE 542; /note=Charge relay system; /evidence=ECO:0000305|PubMed:24398682; ACT_SITE 627; /note=Charge relay system; /evidence=ECO:0000305|PubMed:24398682; ACT_SITE 659; /note=Charge relay system; /evidence=ECO:0000305|PubMed:24398682 |
| 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 except Pro at the P1 position, and has no preference for P2 residues. Shows high dipeptidyl peptidase activity toward the synthetic substrates Lys-Ala-, Gly-Phe-, Met-Leu-, and Ser-Tyr-methylcoumaryl-7-amide (MCA), and slowly hydrolyzes Val-Tyr-MCA. Is likely 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:24398682}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.7, using Lys-Ala-MCA as substrate. {ECO:0000269|PubMed:24398682}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Repeat (3); Signal peptide (1) |
| Keywords | Aminopeptidase;Direct protein sequencing;Hydrolase;Periplasm;Protease;Repeat;Serine protease;Signal;WD repeat |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:24398682}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000269|PubMed:24398682 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 77,455 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=396 uM for Gly-Phe-MCA (at 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:24398682}; KM=688 uM for Lys-Ala-MCA (at 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:24398682}; KM=701 uM for Met-Leu-MCA (at 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:24398682}; KM=151 uM for Lys-Phe-MCA (at 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:24398682}; KM=296 uM for Ser-Tyr-MCA (at 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:24398682}; KM=146 uM for Lys-Leu-MCA (at 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:24398682}; KM=220 uM for Lys-Val-MCA (at 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:24398682}; Note=kcat is 5638 sec(-1) with Gly-Phe-MCA as substrate. kcat is 7577 sec(-1) with Lys-Ala-MCA as substrate. kcat is 5562 sec(-1) with Met-Leu-MCA as substrate. kcat is 744 sec(-1) with Lys-Phe-MCA as substrate. kcat is 1329 sec(-1) with Ser-Tyr-MCA as substrate. kcat is 490 sec(-1) with Lys-Leu-MCA as substrate. kcat is 299 sec(-1) with Lys-Val-MCA as substrate (at 37 degrees Celsius and pH 6.0). {ECO:0000269|PubMed:24398682}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |