| IED ID | IndEnz0002010322 |
| Enzyme Type ID | protease010322 |
| Protein Name |
Dipeptidyl aminopeptidase BI DAP BI EC 3.4.14.- |
| Gene Name | dapb1 |
| Organism | Pseudoxanthomonas mexicana |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Xanthomonadales Xanthomonadaceae Pseudoxanthomonas Pseudoxanthomonas mexicana |
| Enzyme Sequence | MKPTSLLLAATVLMSTPITSALAASATPPDVAKKPHVVKAPHGAERNDEYYWLRDDKRENKEMLAYLNAENAYTDAVMAPLKPLEDKLYDEVVARIKQDDASVPYRERGWWYYARFVTGKDYPVHARRKDGPGVDAVSIQAANAAGDFAGEQVLLDVNALGAGKDYYNVGDYEVSQDNRLLAYADDTNGRRQYTIRFKNLDTGELLPDTVTNAEPNLVWSDDGRTLFYVDKDPETLLSKRVKAHVLGTPASQDALVYEEEDDSFYMGIGRSRDDKFICISVESTVSSEMRCTPAASPGVFTVLAPRERDVEYQADHLGDRWVIRTNADGATNFKIVTAPTDSTSRKDWKDWVAHRDDVFVEGFELFDGFSVVAERANALESLRVIKADGSSDYVKADESAYSMGLSANPETGTDWLRYSYTSMTTPATTYEINTKTGERRQLKQQPVPGYDASKYVTERVWAPARDGKTKIPVTLVYRKDVARDGKAPMLQYAYGSYGASMDPNFSITNVSLLDRGVVYALAHIRGGQEMGRAWYDDGKLYNKINTFTDFIDVTDYLVKEGYAAKDRVAAMGGSAGGLLMGAVSNMAPEKYKVILTLVPFVDVVTTMLDPTIPLTTNEYDEWGNPEEKGYYDYILTYSPYDNLQAKAYPAMFVGTGLWDSQVQYWEPAKYVARLRDLNTGKGPVVFRTNMEAGHGGKSGRFRQYRERAEMFAFMLDQLGVASK |
| Enzyme Length | 723 |
| Uniprot Accession Number | O07834 |
| Absorption | |
| Active Site | ACT_SITE 574; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P24555, ECO:0000255|PROSITE-ProRule:PRU10084"; ACT_SITE 659; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"; ACT_SITE 694; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084" |
| Activity Regulation | ACTIVITY REGULATION: Nearly completely inhibited by 0.5 mM ZnCl(2), 0.1 mM N-tosyl-L-lysyl chloromethyl ketone (TLCK) and 0.1 mM leupeptin. Strongly inhibited by 0.5 mM CoCl(2) and 0.1 mM chymostatin. Activity is hardly affected by general serine protease inhibitors phenylmethanesulfonyl fluoride (PMSF), diisopropyl fluorophosphate (DFP) and N-tosyl-L-phenyl-alanyl chloromethyl ketone (TPCK) or by aspartyl protease inhibitor pepstatin A or by CaCl(2) and EDTA. Cysteine protease inhibitors, such as N-ethylmaleimide (NEM), iodoacetic acid and L-trans-epoxysuccinyl-leucylamido(4-guanido)butane (E-64) have no effect on activity. {ECO:0000269|PubMed:8631703, ECO:0000269|PubMed:9469937}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.14.- |
| Enzyme Function | FUNCTION: Sequentially removes dipeptide units (NH3-P2-P1-) from the amino termini of peptides and proteins. Is able to catalyze the removal of Asp-Arg from the amino termini of angiotensins I and II. Has slight endopeptidase activity on N-terminally blocked peptide derivatives which contain arginine residues at the P1 position. Does not hydrolyze Ala-Ala-Ala and Ala-Ala-Ala-Ala substrates or isulin beta chain. {ECO:0000269|PubMed:8631703}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 35 and 40 degrees Celsius for the hydrolysis of Gly-Arg-pNA. Stable for at least 30 minutes below 20 degrees Celsius.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0 for the hydrolysis of Gly-Arg-pNA. No hydrolysis of Gly-Arg-pNA is detected below pH 5.5 or above pH 11.5. Stable over a broad pH range of between 7.5 and 10.0. {ECO:0000269|PubMed:8631703}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Signal peptide (1) |
| Keywords | Aminopeptidase;Direct protein sequencing;Hydrolase;Protease;Serine protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000269|PubMed:8631703 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 80,754 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.25 mM for Gly-Arg-pNA (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:8631703}; KM=0.019 mM for Arg-Arg-4-methoxy-beta-naphthylamide (Arg-Arg-MNA) (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:8631703}; KM=0.052 mM for Gly-Arg-MNA (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:8631703}; Vmax=195 umol/min/mg enzyme with Gly-Arg-pNA as substrate (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:8631703}; Vmax=145 umol/min/mg enzyme with Arg-Arg-MNA as substrate (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:8631703}; Vmax=95 umol/min/mg enzyme with Gly-Arg-MNA as substrate (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:8631703}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |