| IED ID | IndEnz0002000291 |
| Enzyme Type ID | protease000291 |
| Protein Name |
Xaa-Pro dipeptidase X-Pro dipeptidase EC 3.4.13.9 DFPase Imidodipeptidase Organophosphorus acid anhydrolase 2 OPAA-2 EC 3.1.8.2 Paraoxon hydrolase Phosphotriesterase EC 3.1.8.1 Proline dipeptidase Prolidase |
| Gene Name | pepQ opaA |
| Organism | Alteromonas sp. |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Alteromonadales Alteromonadaceae Alteromonas unclassified Alteromonas Alteromonas sp. |
| Enzyme Sequence | MNKLAVLYAEHIATLQKRTREIIERENLDGVVFHSGQAKRQFLDDMYYPFKVNPQFKAWLPVIDNPHCWIVANGTDKPKLIFYRPVDFWHKVPDEPNEYWADYFDIELLVKPDQVEKLLPYDKARFAYIGEYLEVAQALGFELMNPEPVMNFYHYHRAYKTQYELACMREANKIAVQGHKAARDAFFQGKSEFEIQQAYLLATQHSENDNAYGNIVALNENCAILHYTHFDRVAPATHRSFLIDAGANFNGYAADITRTYDFTGEGEFAELVATMKQHQIALCNQLAPGKLYGELHLDCHQRVAQTLSDFNIVDLSADEIVAKGITSTFFPHGLGHHIGLQVHDVGGFMADEQGAHQEPPEGHPFLRCTRKIEANQVFTIEPGLYFIDSLLGDLAATDNNQHINWDKVAELKPFGGIRIEDNIIVHEDSLENMTRELRARLTTHSLRGLSAPQFSINDPAVMSEYSYPSEPLSYEEEIKKSTFIVHVRTRRILVRRRTLSPILIAVTPMPAITAGLM |
| Enzyme Length | 517 |
| Uniprot Accession Number | Q44238 |
| 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; CATALYTIC ACTIVITY: Reaction=An aryl dialkyl phosphate + H(2)O = dialkyl phosphate + an aryl alcohol.; EC=3.1.8.1; |
| DNA Binding | |
| EC Number | 3.4.13.9; 3.1.8.2; 3.1.8.1 |
| 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 insecticide paraoxon and nerve gases such as diisopropylfluorophosphate (DFP), O-isopropyl methylphosphonofluoridate (sarin), O-pinacolyl methylphosphonofluoridate (soman), and O-cyclohexyl methylphosphonofluoridate. {ECO:0000269|PubMed:10866401, ECO:0000269|PubMed:2001997, ECO:0000269|PubMed:8633861, ECO:0000269|PubMed:9079288}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:2001997, ECO:0000269|PubMed:8633861}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 with DFP as substrate. {ECO:0000269|PubMed:2001997, ECO:0000269|PubMed:8633861}; |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (20); Chain (1); Helix (20); Metal binding (7); Turn (2) |
| Keywords | 3D-structure;Detoxification;Dipeptidase;Hydrolase;Manganese;Metal-binding;Metalloprotease;Protease |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (5) |
| Cross Reference PDB | 3L24; 3L7G; 4ZWO; 4ZWP; 4ZWU; |
| Mapped Pubmed ID | 20000741; 26418828; |
| Motif | |
| Gene Encoded By | |
| Mass | 58,998 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.99 mM for diisopropylfluorophosphate {ECO:0000269|PubMed:2001997, ECO:0000269|PubMed:8633861}; KM=1.57 mM for O-isopropyl methylphosphonofluoridate {ECO:0000269|PubMed:2001997, ECO:0000269|PubMed:8633861}; KM=2.48 mM for O-pinacolyl methylphosphonofluoridate {ECO:0000269|PubMed:2001997, ECO:0000269|PubMed:8633861}; KM=0.63 mM for O-cyclohexyl methylphosphonofluoridate {ECO:0000269|PubMed:2001997, ECO:0000269|PubMed:8633861}; KM=1.27 mM for a chromogenic soman analog {ECO:0000269|PubMed:2001997, ECO:0000269|PubMed:8633861}; Vmax=230 umol/min/mg enzyme with diisopropylfluorophosphate as substrate {ECO:0000269|PubMed:2001997, ECO:0000269|PubMed:8633861}; Vmax=442 umol/min/mg enzyme with O-isopropyl methylphosphonofluoridate as substrate {ECO:0000269|PubMed:2001997, ECO:0000269|PubMed:8633861}; Vmax=151 umol/min/mg enzyme with O-pinacolyl methylphosphonofluoridate as substrate {ECO:0000269|PubMed:2001997, ECO:0000269|PubMed:8633861}; Vmax=652 umol/min/mg enzyme with O-cyclohexyl methylphosphonofluoridate as substrate {ECO:0000269|PubMed:2001997, ECO:0000269|PubMed:8633861}; Vmax=52 umol/min/mg enzyme with a chromogenic soman analog as substrate {ECO:0000269|PubMed:2001997, ECO:0000269|PubMed:8633861}; |
| 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 | 3.1.8.2; |