| IED ID | IndEnz0002011738 |
| Enzyme Type ID | protease011738 |
| Protein Name |
Tetrahedral aminopeptidase TET TET aminopeptidase EC 3.4.11.- Leucyl aminopeptidase PhTET2 |
| Gene Name | frvX PH1527 |
| Organism | Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Thermococci Thermococcales Thermococcaceae Pyrococcus Pyrococcus horikoshii Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) |
| Enzyme Sequence | MEVRNMVDYELLKKVVEAPGVSGYEFLGIRDVVIEEIKDYVDEVKVDKLGNVIAHKKGEGPKVMIAAHMDQIGLMVTHIEKNGFLRVAPIGGVDPKTLIAQRFKVWIDKGKFIYGVGASVPPHIQKPEDRKKAPDWDQIFIDIGAESKEEAEDMGVKIGTVITWDGRLERLGKHRFVSIAFDDRIAVYTILEVAKQLKDAKADVYFVATVQEEVGLRGARTSAFGIEPDYGFAIDVTIAADIPGTPEHKQVTHLGKGTAIKIMDRSVICHPTIVRWLEELAKKHEIPYQLEILLGGGTDAGAIHLTKAGVPTGALSVPARYIHSNTEVVDERDVDATVELMTKALENIHELKI |
| Enzyme Length | 353 |
| Uniprot Accession Number | O59196 |
| Absorption | |
| Active Site | ACT_SITE 212; /note="Proton acceptor"; /evidence="ECO:0000269|PubMed:15375159, ECO:0000269|PubMed:15713475" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA and bestatin in vitro. Is insensitive to papain, antipain, chymostatin, leupeptin, pepstatin and aprotinin. {ECO:0000269|PubMed:15736957}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.11.- |
| Enzyme Function | FUNCTION: Functions as an aminopeptidase, with a clear preference for leucine as the N-terminal amino acid. However, can also cleave moderately long polypeptide substrates of various compositions in a fairly unspecific manner. Has neither carboxypeptidase nor endoproteolytic activities, and it is devoid of N-terminal deblocking activity. Is involved in protein degradation, performing degradation of oligopeptides produced by the proteasome into single amino acids. {ECO:0000269|PubMed:15375159, ECO:0000269|PubMed:15713475, ECO:0000269|PubMed:15736957}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 100 degrees Celsius over a broad pH array. At temperatures lower than 70 degrees Celsius, less than 10% of the maximum activity is detected. Highly thermostable. Shows half-lives of 24.8 minutes and 10.03 hours when incubated at 100 and 80 degrees Celsius, respectively. {ECO:0000269|PubMed:15736957}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 with Leu-pNA as substrate. Strong activity is still detectable at pH 6 and 9. {ECO:0000269|PubMed:15736957}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (18); Chain (1); Helix (14); Metal binding (6); Turn (3) |
| Keywords | 3D-structure;Aminopeptidase;Cobalt;Hydrolase;Metal-binding;Metalloprotease;Protease;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 1XFO; 1Y0R; 1Y0Y; 6F3K; 6R8N; |
| Mapped Pubmed ID | 31217444; |
| Motif | |
| Gene Encoded By | |
| Mass | 39,014 |
| Kinetics | |
| Metal Binding | METAL 68; /note=Zinc 1; METAL 182; /note=Zinc 1; METAL 182; /note=Zinc 2; METAL 213; /note=Zinc 2; METAL 235; /note=Zinc 1; METAL 323; /note=Zinc 2 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.1;3.4.11.B4;3.4.11.B9; |