| IED ID | IndEnz0002015542 |
| Enzyme Type ID | protease015542 |
| Protein Name |
Dipeptidyl aminopeptidase BII DAP BII EC 3.4.14.- |
| Gene Name | dapb2 |
| Organism | Pseudoxanthomonas mexicana |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Xanthomonadales Xanthomonadaceae Pseudoxanthomonas Pseudoxanthomonas mexicana |
| Enzyme Sequence | MRPNLLAAAIAVPLSLLAAQIAQAGEGMWVPQQLPEIAGPLKKAGLKLSPQQISDLTGDPMGAVVALGGCTASFVSPNGLVVTNHHCAYGAIQLNSTAENNLIKNGFNAPTTADEVSAGPNARVFVLDEITDVTKDAKAAIAAAGDDALARTKALEAFEKKLIADCEAEAGFRCRLYSFSGGNTYRLFKNLEIKDVRLAYAPPGSVGKFGGDIDNWMWPRHTGDFAFYRAYVGKDGKPAAFSKDNVPYQPKHWLKFADQPLGAGDFVMVAGYPGSTNRYALAAEFDNTAQWTYPTIARHYKNQIAMVEAAGKQNADIQVKYAATMAGWNNTSKNYDGQLEGFKRIDAAGQKLREEAAVLGWLKGQGAKGQPALDAHAKLLDLLEQSKATRDRDLTLALFNNTAMLGSATQLYRLSIEREKPNAERESGYQERDLPAIEGGLKQLERRYVAAMDRQLQEYWLNEYIKLPADQRVAAVDAWLGGNDAAAVKRALDRLAGTKLGSTEERLKWFAADRKAFEASNDPAIQYAVAVMPTLLKLEQERKTRAGENLAARPVYLQALADYKKSQGEFVYPDANLSLRITFGNVMGYAPKDGMEYTPFTTLEGVVAKETGQDPFDSPKALLDAVAAKRYGGLEDKRIGSVPVNYLSDLDITGGNSGSPVLDAHGKLVGLAFDGNWESVSSNWVFDPKMTRMIAVDGRYLRWIMQEVYPAPQLLKEMNVGK |
| Enzyme Length | 722 |
| Uniprot Accession Number | V5YM14 |
| Absorption | |
| Active Site | ACT_SITE 86; /note="Charge relay system"; /evidence="ECO:0000305|PubMed:24598890, ECO:0000305|PubMed:24827749"; ACT_SITE 224; /note="Charge relay system"; /evidence="ECO:0000305|PubMed:24598890, ECO:0000305|PubMed:24827749"; ACT_SITE 657; /note="Charge relay system"; /evidence="ECO:0000305|PubMed:24598890, ECO:0000305|PubMed:24827749" |
| Activity Regulation | ACTIVITY REGULATION: Completely inhibited by the serine protease inhibitor diisopropyl fluorophosphate (DFP) and potently inhibited by 0.5 mM ZnCl(2), 10 mM o-phenanthlorine, phenylmethanesulfonyl fluoride (PMSF) 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 protease inhibitors, such as chymostatin, leupeptin, N-ethylmaleimide (NEM), iodoacetate (IAA), L-trans-epoxysuccinyl-leucylamido(4-guanido)butane (E64) and pepstatin A or by CoCl(2), CaCl(2) and EDTA. {ECO:0000269|PubMed:8892831}. |
| Binding Site | BINDING 330; /note=Substrate; /evidence=ECO:0000269|PubMed:24827749 |
| 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-) from the free amino termini of oligopeptides and small proteins (PubMed:24598890, PubMed:8892831, PubMed:24827749). Peptide digestion is sequential and substrate recognition is non-specific, with the exception that Pro is not suitable as a P1 residue (PubMed:24827749). Removes many residues of bioactive oligopeptides such as angiotensin I and neuromedin N and cleaves also oxidized insulin B chain. Able to hydrolyze an X-Pro bond, an imido bond. No endopeptidase activity (PubMed:8892831). May play a physiological role in feeding (PubMed:24598890). {ECO:0000269|PubMed:24598890, ECO:0000269|PubMed:24827749, ECO:0000269|PubMed:8892831}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is approximately 30 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 for the hydrolysis of Gly-Phe-pNA. {ECO:0000269|PubMed:8892831}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (18); Binding site (1); Chain (1); Disulfide bond (2); Helix (37); Mutagenesis (16); Region (3); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Aminopeptidase;Direct protein sequencing;Disulfide bond;Hydrolase;Protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000269|PubMed:24598890 |
| Structure 3D | X-ray crystallography (11) |
| Cross Reference PDB | 3WOI; 3WOJ; 3WOK; 3WOL; 3WOM; 3WON; 3WOO; 3WOP; 3WOQ; 3WOR; 4Y06; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 78,698 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.7 mM for Gly-Phe-pNA (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:8892831}; KM=0.87 mM for Ala-Ala-pNA (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:8892831}; KM=7.2 mM for Gly-Phe-beta-naphthylamine (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:8892831}; Vmax=3.4 umol/min/mg enzyme with Gly-Phe-pNA as substrate {ECO:0000269|PubMed:24598890, ECO:0000269|PubMed:24637761}; Vmax=10 umol/min/mg enzyme with Ala-Ala-pNA as substrate {ECO:0000269|PubMed:24598890, ECO:0000269|PubMed:24637761}; Vmax=9.4 umol/min/mg enzyme with Gly-Phe-pNA as substrate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:8892831}; Vmax=20 umol/min/mg enzyme with Ala-Ala-pNA as substrate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:8892831}; Vmax=10 umol/min/mg enzyme with Gly-Phe-beta-naphthylamine as substrate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:8892831}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.6; |