CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.1820 | alpha/beta hydrolase |
Domain Context
CATH Clusters
| Superfamily | alpha/beta hydrolase |
| 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 | 2D5L |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal Structure and Mechanism of Tripeptidyl Activity of Prolyl Tripeptidyl Aminopeptidase from Porphyromonas gingivalis
J.Mol.Biol.
|
