| IED ID | IndEnz0002000315 |
| Enzyme Type ID | protease000315 |
| Protein Name |
Xaa-Pro dipeptidase X-Pro dipeptidase EC 3.4.13.9 Imidodipeptidase Proline dipeptidase Prolidase |
| Gene Name | pepQ b3847 JW3823 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MESLASLYKNHIATLQERTRDALARFKLDALLIHSGELFNVFLDDHPYPFKVNPQFKAWVPVTQVPNCWLLVDGVNKPKLWFYLPVDYWHNVEPLPTSFWTEDVEVIALPKADGIGSLLPAARGNIGYIGPVPERALQLGIEASNINPKGVIDYLHYYRSFKTEYELACMREAQKMAVNGHRAAEEAFRSGMSEFDINIAYLTATGHRDTDVPYSNIVALNEHAAVLHYTKLDHQAPEEMRSFLLDAGAEYNGYAADLTRTWSAKSDNDYAQLVKDVNDEQLALIATMKAGVSYVDYHIQFHQRIAKLLRKHQIITDMSEEAMVENDLTGPFMPHGIGHPLGLQVHDVAGFMQDDSGTHLAAPAKYPYLRCTRILQPGMVLTIEPGIYFIESLLAPWREGQFSKHFNWQKIEALKPFGGIRIEDNVVIHENNVENMTRDLKLA |
| Enzyme Length | 443 |
| Uniprot Accession Number | P21165 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of Xaa-|-Pro dipeptides. Also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.; EC=3.4.13.9; |
| DNA Binding | |
| EC Number | 3.4.13.9 |
| Enzyme Function | FUNCTION: Splits dipeptides with a prolyl residue in the C-terminal position and a polar or nonpolar amino acid at the N-terminal position. With much lower efficiency, also catalyzes the stereoselective hydrolysis of a wide variety of organophosphate triesters and organophosphonate diesters. Is able to hydrolyze the organophosphorus insecticide paraoxon and the p-nitrophenyl analogs of the nerve agents GB (sarin), GD (soman), GF, Vx and rVX. {ECO:0000269|PubMed:15313226}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (19); Chain (1); Frameshift (1); Helix (19); Metal binding (7); Turn (3) |
| Keywords | 3D-structure;Dipeptidase;Direct protein sequencing;Hydrolase;Manganese;Metal-binding;Metalloprotease;Protease;Reference proteome |
| Interact With | P33643 |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4QR8; |
| Mapped Pubmed ID | 15690043; 16606699; 25354344; |
| Motif | |
| Gene Encoded By | |
| Mass | 50,176 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 mM for Ala-Pro {ECO:0000269|PubMed:15313226}; KM=0.10 mM for Arg-Pro {ECO:0000269|PubMed:15313226}; KM=1.4 mM for Gly-Pro {ECO:0000269|PubMed:15313226}; KM=0.15 mM for His-Pro {ECO:0000269|PubMed:15313226}; KM=0.10 mM for Ile-Pro {ECO:0000269|PubMed:15313226}; KM=1.0 mM for Leu-Pro {ECO:0000269|PubMed:15313226}; KM=0.27 mM for Lys-Pro {ECO:0000269|PubMed:15313226}; KM=0.13 mM for Met-Pro {ECO:0000269|PubMed:15313226}; KM=0.43 mM for Phe-Pro {ECO:0000269|PubMed:15313226}; KM=0.31 mM for Pro-Pro {ECO:0000269|PubMed:15313226}; KM=0.46 mM for Ser-Pro {ECO:0000269|PubMed:15313226}; KM=0.16 mM for Tyr-Pro {ECO:0000269|PubMed:15313226}; KM=0.40 mM for Val-Pro {ECO:0000269|PubMed:15313226}; KM=38 mM for diisopropylfluorophosphate {ECO:0000269|PubMed:15313226}; Note=Among the dipeptides described above, the highest catalytic efficiency is observed with dipeptides containing charge residues.; |
| Metal Binding | METAL 246; /note=Manganese 2; /evidence=ECO:0000250; METAL 257; /note=Manganese 1; /evidence=ECO:0000250; METAL 257; /note=Manganese 2; /evidence=ECO:0000250; METAL 339; /note=Manganese 1; /evidence=ECO:0000250; METAL 384; /note=Manganese 1; /evidence=ECO:0000250; METAL 423; /note=Manganese 1; /evidence=ECO:0000250; METAL 423; /note=Manganese 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |