Home  |  Contact

A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.

ENZYME entry: EC

Accepted Name
Xaa-Xaa-Pro tripeptidyl-peptidase.
Alternative Name(s)
Prolyl tripeptidyl peptidase.
Prolyltripeptidyl amino peptidase.
Prolyltripeptidyl aminopeptidase.
Reaction catalysed
Hydrolysis of Xaa-Xaa-Pro-|-Yaa- releasing the N-terminal tripeptide of a peptide with Pro as the third residue (position P1) and where Yaa is not proline
  • This cell-surface-associated serine exopeptidase is found in the Gram-negative, anaerobic bacterium Porphyromonas gingivalis, which has been implicated in adult periodontal disease.
  • The enzyme releases tripeptides from the free amino terminus of peptides and small proteins, such as interleukin-6.
  • The enzyme possesses an absolute requirement for a proline residue at the P1 position but is completely inactivated by a proline residue at the P1' position.
  • The size of the peptide does not affect the rate of reaction.
PRIAM enzyme-specific profiles3.4.14.12
KEGG Ligand Database for Enzyme Nomenclature3.4.14.12
IUBMB Enzyme Nomenclature3.4.14.12
MEDLINEFind literature relating to

View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.4.14.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.4.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-