O59196 · TET_PYRHO
- ProteinTetrahedral aminopeptidase
- GenefrvX
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids353 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Miscellaneous
The hydrolytic mechanism is nonprocessive. Therefore, the enzyme does not process one substrate molecule completely before starting with another one. Instead, the reaction products are generated by multiple rounds of substrate digestion.
Cofactor
Co2+ (UniProtKB | Rhea| CHEBI:48828 )
Note: Binds 2 Zn2+ ions per subunit. Can also use Co2+.
Activity regulation
Inhibited by EDTA and bestatin in vitro. Is insensitive to papain, antipain, chymostatin, leupeptin, pepstatin and aprotinin.
pH Dependence
Optimum pH is 7.5 with Leu-pNA as substrate. Strong activity is still detectable at pH 6 and 9.
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.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 68 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 182 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 182 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Active site | 212 | Proton acceptor | |||
Binding site | 213 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 235 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 323 | Zn2+ 2 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | aminopeptidase activity | |
Molecular Function | metal ion binding | |
Molecular Function | metallopeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameTetrahedral aminopeptidase
- EC number
- Short namesTET; TET aminopeptidase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Thermococci > Thermococcales > Thermococcaceae > Pyrococcus
Accessions
- Primary accessionO59196
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000391012 | 1-353 | Tetrahedral aminopeptidase | ||
Interaction
Subunit
Homododecamer. The assembly of six dimers results in a tetrahedral-shaped structure; all 12 active sites are located on the inside of the tetrahedron. Substrate access is granted by four pores with a maximal diameter of 18 Angstroms, allowing only small peptides and unfolded proteins access to the active site. Beside the four entry ports, TET contains 12 small product release openings, which are large enough to allow passage of only single amino acid residues.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length353
- Mass (Da)39,014
- Last updated1998-08-01 v1
- ChecksumA6AE25809C8B2041
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BA000001 EMBL· GenBank· DDBJ | BAA30637.1 EMBL· GenBank· DDBJ | Genomic DNA |