| IED ID | IndEnz0002016267 |
| Enzyme Type ID | protease016267 |
| Protein Name |
Dipeptidyl aminopeptidase 4 EC 3.4.14.5 Dipeptidyl aminopeptidase IV DAP IV |
| Gene Name | dap4 |
| Organism | Pseudoxanthomonas mexicana |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Xanthomonadales Xanthomonadaceae Pseudoxanthomonas Pseudoxanthomonas mexicana |
| Enzyme Sequence | MRLALFALFALMTVATALPAHAEKLTLEAITGSAPLSGPTLTKPQIAPDGSRVTFLRGKDRDRNRLDLWEYDIASGQTRLLVDSSVVLPGEEVLSDEEKARRERQRIAALSGIVDYQWSPDGKALLFPLGGELYFYDLTKSGRDAVRKLTNGGGFATDPKISPKGGFVSFIRDRNLWAIDLASGKEVQLTRDGSDTIGNGVAEFVADEEMDRHTGYWWAPDDAAIAFARIDETPVPVQKRYEVYPDRTEVVEQRYPAAGDHNVRVQLGVIAPKTGARPRWIDLGKDPDIYLARVDWRDPQRLTFQRQSRDQKKIELIETTLTNGTQRTLVTETSTTWVPLHNDLRFLKDGRFLWSSERSGFEHLYVASEDGSTLTALTQGEWVVDSLLAIDEAAGLAYVSGTRDGATEAHVYAVPLSGGEPRRLTQAPGMHAATFARNASVFVDSWSSDTTLPQIELFKADGTKLATLLVNDVSDATHPYAKYRAAHQPTAYGTLTAADGTTPLHYSLIKPAGFDPKKQYPVVVFVYGGPAAQTVTRAWPGRSDSFFNQYLAQQGYVVFTLDNRGTPRRGAAFGGALYGKQGTVEVDDQLRGIEWLKSQAFVDPARIGVYGWSNGGYMTLMLLAKHDEAYACGVAGAPVTDWALYDTHYTERYMDLPKANEAGYREASVFTHVDGIGAGKLLLIHGMADDNVLFTNSTKLMSELQKRGTPFELMTYPGAKHGLRGSDLLHRYRLTEDFFARCLKP |
| Enzyme Length | 745 |
| Uniprot Accession Number | Q6F3I7 |
| Absorption | |
| Active Site | ACT_SITE 613; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:Q12884, ECO:0000255|PROSITE-ProRule:PRU10084"; ACT_SITE 689; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:Q12884"; ACT_SITE 721; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:Q12884" |
| Activity Regulation | ACTIVITY REGULATION: Completely inhibited by the serine protease inhibitor diisopropyl fluorophosphate (DFP) and moderately by N-tosyl-L-phenyl-alanyl chloromethyl ketone (TPCK). Somewhat inhibited by phenylmethanesulfonyl fluoride (PMSF). Activity is not affected by thiol- or metalloprotease inhibitors, such as iodoacetate (IAA), EDTA, N-tosyl-L-lysyl chloromethyl ketone (TLCK), o-phenanthlorine, N-ethylmaleimide (NEM) or dithiothreitol (DTT). {ECO:0000269|PubMed:8988635}. |
| Binding Site | BINDING 208; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q12884; BINDING 209; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q12884 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.; EC=3.4.14.5; Evidence={ECO:0000269|PubMed:15866709, ECO:0000269|PubMed:8988635}; |
| DNA Binding | |
| EC Number | 3.4.14.5 |
| Enzyme Function | FUNCTION: Catalyzes the sequential release of Tyr-Pro, Phe-Pro and Gly-Pro from the N-terminus of peptides and proteins. Is able to cleaves bioactive peptide beta-casomorphin. {ECO:0000269|PubMed:8988635}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 40 and 50 degrees Celsius for the hydrolysis of Gly-Pro-pNA. Stable for at least 30 min below 30 degrees Celsius. {ECO:0000269|PubMed:8988635}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 for the hydrolysis of Gly-Pro-pNA. No hydrolysis is detected at a pH below 5.5 or above 11.0. {ECO:0000269|PubMed:8988635}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (1); Beta strand (48); Binding site (2); Chain (1); Helix (19); Initiator methionine (1); Mutagenesis (2); Sequence conflict (1); Signal peptide (1); Turn (8) |
| Keywords | 3D-structure;Alternative initiation;Aminopeptidase;Cytoplasm;Direct protein sequencing;Hydrolase;Periplasm;Protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:15866709}.; SUBCELLULAR LOCATION: [Isoform 1]: Periplasm {ECO:0000269|PubMed:15866709}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..22; /evidence="ECO:0000269|PubMed:15866709, ECO:0000269|PubMed:8988635" |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 5YP1; 5YP2; 5YP3; 5YP4; |
| Mapped Pubmed ID | 29426867; |
| Motif | |
| Gene Encoded By | |
| Mass | 82,295 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.142 mM for Gly-Pro-pNA (at pH 8.0 and 37 degrees Celsius) {ECO:0000269|PubMed:8988635}; Vmax=16.7 umol/min/mg enzyme with Gly-Pro-pNA as substrate (at pH 8.0 and 37 degrees Celsius) {ECO:0000269|PubMed:8988635}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.14.5; |