| IED ID | IndEnz0002016722 |
| Enzyme Type ID | protease016722 |
| Protein Name |
Lysyl aminopeptidase EC 3.4.11.15 |
| Gene Name | PF1861 |
| 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 | MVDWELMKKIIESPGVSGYEHLGIRDLVVDILKDVADEVKIDKLGNVIAHFKGSAPKVMVAAHMDKIGLMVNHIDKDGYLRVVPIGGVLPETLIAQKIRFFTEKGERYGVVGVLPPHLRREAKDQGGKIDWDSIIVDVGASSREEAEEMGFRIGTIGEFAPNFTRLSEHRFATPYLDDRICLYAMIEAARQLGEHEADIYIVASVQEEIGLRGARVASFAIDPEVGIAMDVTFAKQPNDKGKIVPELGKGPVMDVGPNINPKLRQFADEVAKKYEIPLQVEPSPRPTGTDANVMQINREGVATAVLSIPIRYMHSQVELADARDVDNTIKLAKALLEELKPMDFTP |
| Enzyme Length | 346 |
| Uniprot Accession Number | Q8TZW4 |
| Absorption | |
| Active Site | ACT_SITE 207; /note=Proton acceptor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferentially, release of N-terminal lysine.; EC=3.4.11.15; Evidence={ECO:0000269|PubMed:15743956}; |
| DNA Binding | |
| EC Number | 3.4.11.15 |
| Enzyme Function | FUNCTION: Hydrolyzes di-, tri- and tetrapeptides with a lysine as the N-terminal amino acid and with Gly, Lys, Ala, Phe or Glu in the second position. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 100 degrees Celsius. {ECO:0000269|PubMed:15743956}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:15743956}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (17); Chain (1); Helix (11); Metal binding (6); Turn (3) |
| Keywords | 3D-structure;Aminopeptidase;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4X8I; |
| Mapped Pubmed ID | 26853450; |
| Motif | |
| Gene Encoded By | |
| Mass | 38,214 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.6 mM for Lys-pNA {ECO:0000269|PubMed:15743956}; KM=1.8 mM for Lys-Gly-Gly {ECO:0000269|PubMed:15743956}; KM=1.4 mM for Arg-pNA {ECO:0000269|PubMed:15743956}; Vmax=2900 umol/min/mg enzyme with Lys-pNA as substrate {ECO:0000269|PubMed:15743956}; Vmax=2300 umol/min/mg enzyme with Lys-Gly-Gly as substrate {ECO:0000269|PubMed:15743956}; Vmax=1200 umol/min/mg enzyme with Arg-pNA as substrate {ECO:0000269|PubMed:15743956}; |
| Metal Binding | METAL 63; /note=Zinc 1; /evidence=ECO:0000250; METAL 177; /note=Zinc 1; /evidence=ECO:0000250; METAL 177; /note=Zinc 2; /evidence=ECO:0000250; METAL 208; /note=Zinc 2; /evidence=ECO:0000250; METAL 230; /note=Zinc 1; /evidence=ECO:0000250; METAL 314; /note=Zinc 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.15; |