| IED ID | IndEnz0002000337 |
| Enzyme Type ID | protease000337 |
| Protein Name |
Xaa-Pro dipeptidase X-Pro dipeptidase EC 3.4.13.9 DFPase Imidodipeptidase Organophosphorus acid anhydrolase OPAA EC 3.1.8.2 Proline dipeptidase Prolidase |
| Gene Name | pepQ opa |
| Organism | Pseudoalteromonas haloplanktis (Alteromonas haloplanktis) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Alteromonadales Pseudoalteromonadaceae Pseudoalteromonas Pseudoalteromonas haloplanktis (Alteromonas haloplanktis) |
| Enzyme Sequence | MEKLAVLYAEHIATLQQRTRTICEQEGLEGLVIHSGQAKRQFLDDMYYPFKVNPHFKAWLPVIDNPHCWIVVNGSDKPKLIFYRPIDFWHKVPDEPRDFWAEYFDIELLLQPDQVEKLLPYDKAKFAYIGEYLEVAQALGFSIMNPEPVLNYIHYHRAYKTQYELECLRNANRIAVDGHKAARDAFFNGGSEFDIQQAYLMATRQSENEMPYGNIVALNENCAILHYTHFEPKAPQTHNSFLIDAGANFNGYAADITRTYDFKKQGEFADLVNAMTAHQIELGKSLKPGLLYGDLHIDCHNRIAQLLSDFDIVKLPAAEIVERQITSTFFPHGLGHHLGAQVHDVGGFMRDETGAHQAPPEGHPFLRCTRLIEKNQVFTIEPGLYFIDSLLGDLAQTDNKQFINWEKVEAFKPFGGIRIEDNIIVHEDSLENMTRNLLLD |
| Enzyme Length | 440 |
| Uniprot Accession Number | P77814 |
| 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; CATALYTIC ACTIVITY: Reaction=diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride + 2 H(+); Xref=Rhea:RHEA:24100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17051, ChEBI:CHEBI:17941, ChEBI:CHEBI:57896; EC=3.1.8.2; |
| DNA Binding | |
| EC Number | 3.4.13.9; 3.1.8.2 |
| Enzyme Function | FUNCTION: Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position and a nonpolar amino acid at the N-terminal position. Also catalyzes the hydrolysis of toxic organophosphorus cholinesterase-inhibiting compounds including nerve gases such as diisopropylfluorophosphate (DFP), O-isopropyl methylphosphonofluoridate (sarin), O-pinacolyl methylphosphonofluoridate (soman), and O-cyclohexyl methylphosphonofluoridate. {ECO:0000269|PubMed:9079288}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:9079288}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:9079288}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Metal binding (7) |
| Keywords | Detoxification;Dipeptidase;Direct protein sequencing;Hydrolase;Manganese;Metal-binding;Metalloprotease;Protease |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus is blocked. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 50,481 |
| Kinetics | |
| Metal Binding | METAL 244; /note=Manganese 2; /evidence=ECO:0000250; METAL 255; /note=Manganese 1; /evidence=ECO:0000250; METAL 255; /note=Manganese 2; /evidence=ECO:0000250; METAL 336; /note=Manganese 1; /evidence=ECO:0000250; METAL 381; /note=Manganese 1; /evidence=ECO:0000250; METAL 420; /note=Manganese 1; /evidence=ECO:0000250; METAL 420; /note=Manganese 2; /evidence=ECO:0000250 |
| Rhea ID | RHEA:24100 |
| Cross Reference Brenda |