O59196 · TET_PYRHO

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

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

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
IDPosition(s)Description
Binding site68Zn2+ 1 (UniProtKB | ChEBI)
Binding site182Zn2+ 1 (UniProtKB | ChEBI)
Binding site182Zn2+ 2 (UniProtKB | ChEBI)
Active site212Proton acceptor
Binding site213Zn2+ 2 (UniProtKB | ChEBI)
Binding site235Zn2+ 1 (UniProtKB | ChEBI)
Binding site323Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionaminopeptidase activity
Molecular Functionmetal ion binding
Molecular Functionmetallopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Tetrahedral aminopeptidase
  • EC number
  • Short names
    TET; TET aminopeptidase
  • Alternative names
    • Leucyl aminopeptidase
    • PhTET2

Gene names

    • Name
      frvX
    • Ordered locus names
      PH1527

Organism names

Accessions

  • Primary accession
    O59196

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003910121-353Tetrahedral 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

Family & Domains

Sequence similarities

Belongs to the peptidase M42 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    353
  • Mass (Da)
    39,014
  • Last updated
    1998-08-01 v1
  • Checksum
    A6AE25809C8B2041
MEVRNMVDYELLKKVVEAPGVSGYEFLGIRDVVIEEIKDYVDEVKVDKLGNVIAHKKGEGPKVMIAAHMDQIGLMVTHIEKNGFLRVAPIGGVDPKTLIAQRFKVWIDKGKFIYGVGASVPPHIQKPEDRKKAPDWDQIFIDIGAESKEEAEDMGVKIGTVITWDGRLERLGKHRFVSIAFDDRIAVYTILEVAKQLKDAKADVYFVATVQEEVGLRGARTSAFGIEPDYGFAIDVTIAADIPGTPEHKQVTHLGKGTAIKIMDRSVICHPTIVRWLEELAKKHEIPYQLEILLGGGTDAGAIHLTKAGVPTGALSVPARYIHSNTEVVDERDVDATVELMTKALENIHELKI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BA000001
EMBL· GenBank· DDBJ
BAA30637.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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