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 | 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
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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
J.Mol.Biol.
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