IED ID | IndEnz0002019027 |
Enzyme Type ID | protease019027 |
Protein Name |
Dipeptidyl-peptidase 7 DPP-7 DPP7 EC 3.4.14.- |
Gene Name | dpp7 dpp-7 PGN_1479 |
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 | MQMKLKSILLGAALLLGASGVAKADKGMWLLNELNQENLDRMRELGFTLPLDSLYSFDKPSIANAVVIFGGGCTGITVSDQGLIFTNHHCGYGAIQSQSTVDHDYLRDGFVSRTMGEELPIPGLSVKYLRKIVKVTDKVEGQLKGITDEMERLRKAQEVCQELAKKENADENQLCIVEPFYSNNEYFLIVYDVFKDVRMVFAPPSSVGKFGGDTDNWMWPRHTGDFSVFRVYAGADNRPAEYSKDNKPYKPVYFAAVSMQGYKADDYAMTIGFPGSTDRYLTSWGVEDRIENENNPRIEVRGIKQGIWKEAMSADQATRIKYASKYAQSANYWKNSIGMNRGLARLDVIGRKRAEERAFADWIRKNGKSAVYGDVLSSLEKAYKEGAKANREMTYLSETLFGGTEVVRFAQFANALATNPDAHAGILKSLDDKYKDYLPSLDRKVLPAMLDIVRRRIPADKLPDIFKNVIDKKFKGDTKKYADFVFDKSVVPYSDKFHAMLKSMDKEKFAKAIEKDPAVELSKSVIAAARAIQADAMANAYAIEKGKRLFFAGLREMYPGRALPSDANFTMRMSYGSIKGYEPQDGAWYNYHTTGKGVLEKQDPKSDEFAVQENILDLFRTKNYGRYAENGQLHIAFLSNNDITGGNSGSPVFDKNGRLIGLAFDGNWEAMSGDIEFEPDLQRTISVDIRYVLFMIDKWGQCPRLIQELKLI |
Enzyme Length | 712 |
Uniprot Accession Number | B2RKV3 |
Absorption | |
Active Site | ACT_SITE 89; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:V5YM14; ACT_SITE 225; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:V5YM14; ACT_SITE 648; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:V5YM14 |
Activity Regulation | ACTIVITY REGULATION: Is inhibited in vitro by typical serine protease inhibitors like diisopropyl fluorophosphate, Pefablock, and 3,4-dichloroisocoumarin, but not by typical cysteine class inhibitors such as E-64 or iododoacetic acid. {ECO:0000269|PubMed:11096098}. |
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 (PubMed:11096098, PubMed:23246913). Shows a broad specificity for both aliphatic and aromatic residues in the P1 position, with glycine or proline being not acceptable in this position (PubMed:11096098). Most potently cleaves the synthetic substrate Met-Leu-methylcoumaryl-7-amide (Met-Leu-MCA), Leu-Arg-MCA and Lys-Ala-MCA to a lesser extent (PubMed:23246913). 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 (PubMed:11096098). {ECO:0000269|PubMed:11096098, ECO:0000269|PubMed:23246913}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 43 degrees Celsius, using Ala-Phe-pNA as substrate. {ECO:0000269|PubMed:11096098}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Is active against Ala-Phe-pNA over a broad pH range, from neutral to basic pH (6.5-9.0). {ECO:0000269|PubMed:11096098}; |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Coiled coil (1); Mutagenesis (3); Signal peptide (1); Site (1) |
Keywords | Aminopeptidase;Cell outer membrane;Coiled coil;Direct protein sequencing;Hydrolase;Membrane;Protease;Serine protease;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:11096098}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000269|PubMed:11096098 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 80,107 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=313 uM for Ala-Ala-pNA {ECO:0000269|PubMed:11096098}; KM=441 uM for Ala-Phe-pNA {ECO:0000269|PubMed:11096098}; KM=256 uM for Gly-Ala-pNA {ECO:0000269|PubMed:11096098}; |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |