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; |