| IED ID | IndEnz0002000339 |
| Enzyme Type ID | protease000339 |
| Protein Name |
Xaa-Pro dipeptidase X-Pro dipeptidase EC 3.4.13.9 Imidodipeptidase Proline dipeptidase Prolidase |
| Gene Name | pepQ PF1343 |
| Organism | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Thermococci Thermococcales Thermococcaceae Pyrococcus Pyrococcus furiosus Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
| Enzyme Sequence | MKERLEKLVKFMDENSIDRVFIAKPVNVYYFSGTSPLGGGYIIVDGDEATLYVPELEYEMAKEESKLPVVKFKKFDEIYEILKNTETLGIEGTLSYSMVENFKEKSNVKEFKKIDDVIKDLRIIKTKEEIEIIEKACEIADKAVMAAIEEITEGKREREVAAKVEYLMKMNGAEKPAFDTIIASGHRSALPHGVASDKRIERGDLVVIDLGALYNHYNSDITRTIVVGSPNEKQREIYEIVLEAQKRAVEAAKPGMTAKELDSIAREIIKEYGYGDYFIHSLGHGVGLEIHEWPRISQYDETVLKEGMVITIEPGIYIPKLGGVRIEDTVLITENGAKRLTKTERELL |
| Enzyme Length | 348 |
| Uniprot Accession Number | P81535 |
| 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 in the C-terminal position and a nonpolar amino acid at the N-terminal position. {ECO:0000269|PubMed:9733678}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 100 degrees Celsius. Highly thermostable. {ECO:0000269|PubMed:9733678}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:9733678}; |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (18); Chain (1); Helix (13); Metal binding (7); Mutagenesis (3); Turn (2) |
| Keywords | 3D-structure;Cobalt;Cytoplasm;Dipeptidase;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1PV9; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 39,387 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.8 mM for Met-Pro {ECO:0000269|PubMed:9733678}; KM=3 mM for Leu-Pro {ECO:0000269|PubMed:9733678}; KM=4.2 mM for Val-Pro {ECO:0000269|PubMed:9733678}; KM=8.3 mM for Ala-Pro {ECO:0000269|PubMed:9733678}; KM=20 mM for Phe-Pro {ECO:0000269|PubMed:9733678}; Vmax=645 umol/min/mg enzyme with Met-Pro as substrate {ECO:0000269|PubMed:9733678}; Vmax=645 umol/min/mg enzyme with Leu-Pro as substrate {ECO:0000269|PubMed:9733678}; Vmax=175 umol/min/mg enzyme with Val-Pro as substrate {ECO:0000269|PubMed:9733678}; Vmax=250 umol/min/mg enzyme with Ala-Pro as substrate {ECO:0000269|PubMed:9733678}; Vmax=1000 umol/min/mg enzyme with Phe-Pro as substrate {ECO:0000269|PubMed:9733678}; |
| Metal Binding | METAL 209; /note=Cobalt 2; METAL 220; /note=Cobalt 1; METAL 220; /note=Cobalt 2; METAL 284; /note=Cobalt 1; METAL 313; /note=Cobalt 1; METAL 327; /note=Cobalt 1; METAL 327; /note=Cobalt 2 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.13.9; |