| IED ID | IndEnz0002006028 |
| Enzyme Type ID | protease006028 |
| Protein Name |
Dipeptidyl aminopeptidase BIII DAP BIII EC 3.4.14.- |
| Gene Name | dapb3 |
| Organism | Pseudoxanthomonas mexicana |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Xanthomonadales Xanthomonadaceae Pseudoxanthomonas Pseudoxanthomonas mexicana |
| Enzyme Sequence | MRHPAFRLTLLASTVAFALAPQAAQAAPSAADRIAGTELIARDALFGNPERANVQISPDGKYLSWVAAVDGVLNVWIAPADNPSQARAVTQDTARGIRSYFWSYQPDTLLYLRDSGGDEDFHLYAVDLKTGQAKDLTPFPKTTAQVAGVSPKHPGTILVGMNDRDAQWHDIYKVDLASGNRTLLEKNDAQIAGYIADADYTLKYAQRSRPDGGADVLRRGANGAWEKFDDIPFEDVLTTSPGGLTLDGKTLYFTDSRGRNTAALFAIDVASGKRTLVLEDARADVGGTLADPATGKVQAVSVDYLRDEWKVVDPAIRADLEKLEAIGPGDVSVNTRTLDDKTWIVAYSAAEAPLVYYRYDRSAGTLTKLFSARPKLEGKPLVPQWPVEIASRDNKTLVSYLTLPRSADANNDGKADAPVPLVLLVHGGPWARDSYGYGGYNQWLANRGYAVLSVNFRGSTGFGKDFTNAGNGEWAGKMHDDLIDAVQWAVKQGVTTQDQVAIMGGSYGGYATLTGLTFTPDAFACGVDIVGPSNLNTLLSTVPPYWASFFEQLAKRMGDPRTDAGKKWLTERSPLTRADQIKKPLLIGQGANDPRVKQAESDQIVKAMQAKNIPVTYVLFPDEGHGFARPENNKAFNAVTEGFLAQCLGGRAEPIGKDFTGSSISVPVGADGVPGLAEALKGHTQEVKK |
| Enzyme Length | 689 |
| Uniprot Accession Number | V5YMB3 |
| Absorption | |
| Active Site | ACT_SITE 506; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P13798, ECO:0000255|PROSITE-ProRule:PRU10084"; ACT_SITE 593; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"; ACT_SITE 625; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P13798, ECO:0000255|PROSITE-ProRule:PRU10084" |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by the serine protease inhibitor diisopropyl fluorophosphate (DFP), chymostatin, leupeptin, 0.5 mM ZnCl(2), 10 mM o-phenanthlorine and N-tosyl-L-phenyl-alanyl chloromethyl ketone (TPCK), but not by N-tosyl-L-lysyl chloromethyl ketone (TLCK). Activity is not affected significantly by iodoacetate (IAA), L-trans-epoxysuccinyl-leucylamido(4-guanido)butane (E64), pepstatin A and phenylmethanesulfonyl fluoride (PMSF). Activity is stimulated by addition of 0.5 mM CaCl(2), 10 mM EDTA and N-ethylmaleimide (NEM). {ECO:0000269|PubMed:8892831}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.14.- |
| Enzyme Function | FUNCTION: Exopeptidase that catalyzes the removal of dipeptide units (NH2-P2-P1- or -P1'-P2'-COOH) from the free amino or carboxy termini. Prefers substrates composed of bulky, hydrophobic amino acids at P1 and P1' positions. Has endopeptidase activity on N-terminally blocked peptide derivatives which contain aromatic amino acid residue at the P1 position. Exopeptidase activity is much higher than its endopeptidase activity. {ECO:0000269|PubMed:8892831}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 35 and 40 degrees Celsius for the hydrolysis of Gly-Phe-pNA. Stable at a temperature below 20 degrees Celsius for 30 minutes. {ECO:0000269|PubMed:8892831}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 to 9.0 for the hydrolysis of Gly-Phe-pNA. {ECO:0000269|PubMed:8892831}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Signal peptide (1) |
| Keywords | Aminopeptidase;Hydrolase;Protease;Serine protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 74,228 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.33 mM for Gly-Phe-pNA (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:8892831}; KM=1.0 mM for Gly-Phe-beta-naphthylamine (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:8892831}; Vmax=9.6 umol/min/mg enzyme with Gly-Phe-pNA as substrate (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:8892831}; Vmax=330 umol/min/mg enzyme with Gly-Phe-beta-naphthylamine as substrate (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:8892831}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |