CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.140 | 8 Propeller |
|
2.140.10 | Methanol Dehydrogenase; Chain A |
|
2.140.10.30 | Dipeptidylpeptidase IV, N-terminal domain |
Domain Context
CATH Clusters
| Superfamily | 2.140.10.30 |
| Functional Family | Dipeptidyl peptidase IV |
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.
|
| 3.4.14.5 |
Dipeptidyl-peptidase IV.
based on mapping to UniProt Q7MUW6
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.
-!- A membrane-bound serine-type peptidase in mammals. -!- EC 3.4.14.11 catalyzes a similar reaction. -!- Belongs to peptidase family S9B.
|
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.
|