(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Proteobacteria: NE > Gammaproteobacteria: NE > Xanthomonadales: NE > Xanthomonadaceae: NE > Pseudoxanthomonas: NE > Pseudoxanthomonas mexicana: NE
Molecular evidence
Database
No mutation 4 structures(e.g. : 5YP1, 5YP2, 5YP3... more)(less) 5YP1: Crystal structure of dipeptidyl peptidase IV (DPP IV) from Pseudoxanthomonas mexicana WO24, 5YP2: Crystal structure of dipeptidyl peptidase IV (DPP IV) with DPP4 inhibitor from Pseudoxanthomonas mexicana WO24, 5YP3: Crystal structure of dipeptidyl peptidase IV (DPP IV) with Ile-Pro from Pseudoxanthomonas mexicana, 5YP4: Crystal structure of dipeptidyl peptidase IV (DPP IV) with Lys-Pro from Pseudoxanthomonas mexicana WO24 No kinetic
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MRLALFALFALMTVATALPAHAEKLTLEAITGSAPLSGPTLTKPQIAPDG SRVTFLRGKDRDRNRLDLWEYDIASGQTRLLVDSSVVLPGEEVLSDEEKA RRERQRIAALSGIVDYQWSPDGKALLFPLGGELYFYDLTKSGRDAVRKLT NGGGFATDPKISPKGGFVSFIRDRNLWAIDLASGKEVQLTRDGSDTIGNG VAEFVADEEMDRHTGYWWAPDDAAIAFARIDETPVPVQKRYEVYPDRTEV VEQRYPAAGDHNVRVQLGVIAPKTGARPRWIDLGKDPDIYLARVDWRDPQ RLTFQRQSRDQKKIELIETTLTNGTQRTLVTETSTTWVPLHNDLRFLKDG RFLWSSERSGFEHLYVASEDGSTLTALTQGEWVVDSLLAIDEAAGLAYVS GTRDGATEAHVYAVPLSGGEPRRLTQAPGMHAATFARNASVFVDSWSSDT TLPQIELFKADGTKLATLLVNDVSDATHPYAKYRAAHQPTAYGTLTAADG TTPLHYSLIKPAGFDPKKQYPVVVFVYGGPAAQTVTRAWPGRSDSFFNQY LAQQGYVVFTLDNRGTPRRGAAFGGALYGKQGTVEVDDQLRGIEWLKSQA FVDPARIGVYGWSNGGYMTLMLLAKHDEAYACGVAGAPVTDWALYDTHYT ERYMDLPKANEAGYREASVFTHVDGIGAGKLLLIHGMADDNVLFTNSTKL MSELQKRGTPFELMTYPGAKHGLRGSDLLHRYRLTEDFFARCLKP
Dipeptidyl peptidase IV (DPP IV, DPP4, or DAP IV) preferentially cleaves substrate peptides with Pro or Ala at the P1 position. The substrate recognition mechanism has been fully elucidated for mammalian DPP IV by crystal structure analyses but not for bacterial orthologues. Here, we report the crystal structures of a bacterial DPP IV (PmDAP IV) in its free form and in complexes with two kinds of dipeptides as well as with a non-peptidyl inhibitor at 1.90 to 2.47 A resolution. Acyl-enzyme intermediates were observed for the dipeptide complexes of PmDAP IV, whereas tetrahedral intermediates were reported for the oligopeptide complexes of mammalian DPP IVs. This variation reflects the different structural environments of the active site Arg residues, which are involved in the recognition of a substrate carbonyl group, of mammalian and bacterial enzymes. A phylogenetic analysis revealed that PmDAP IV is a closer relative of dipeptidyl peptidases 8 and 9 (DPP8 and DPP9, DPP IV-family enzymes) than DPP IV. These results provide new insights into the substrate recognition mechanism of bacterial DAP IVs and may assist in the development of selective inhibitors for DAP IVs from pathogenic asaccharolytic bacteria, which utilise proteins or peptides as an energy source.
Dipeptidyl aminopeptidase IV (DAP IV or DPP IV) from Pseudoxanthomonas mexicana WO24 (PmDAP IV) preferentially cleaves substrate peptides with Pro or Ala at the P1 position [NH2-P2-P1(Pro/Ala)-P1'-P2'...]. For crystallographic studies, the periplasmic form of PmDAP IV was overproduced in Escherichia coli, purified and crystallized in complex with the tripeptide Lys-Pro-Tyr using the hanging-drop vapour-diffusion method. Kinetic parameters of the purified enzyme against a synthetic substrate were also determined. X-ray diffraction data to 1.90 A resolution were collected from a triclinic crystal form belonging to space group P1, with unit-cell parameters a = 88.66, b = 104.49, c = 112.84 A, alpha = 67.42, beta = 68.83, gamma = 65.46 degrees . Initial phases were determined by the molecular-replacement method using Stenotrophomonas maltophilia DPP IV (PDB entry 2ecf) as a template and refinement of the structure is in progress.
Pseudomonas sp. WO24 dipeptidyl aminopeptidase IV
