CATH Classification

Domain Context

CATH Clusters

Superfamily Dipeptidylpeptidase IV, N-terminal domain
Functional Family

Enzyme Information

3.4.14.12
Xaa-Xaa-Pro tripeptidyl-peptidase.
based on mapping to UniProt Q7MUW6
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.

UniProtKB Entries (1)

Q7MUW6
PTP_PORGI
Porphyromonas gingivalis W83
Prolyl tripeptidyl peptidase

PDB Structure

PDB 2Z3W
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Novel inhibitor for prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis and details of substrate-recognition mechanism
Xu, Y., Nakajima, Y., Ito, K., Zheng, H., Oyama, H., Heiser, U., Hoffmann, T., Gartner, U.T., Demuth, H.U., Yoshimoto, T.
J.Mol.Biol.