ENZYME entry: EC 3.4.14.12
| Accepted Name |
|---|
| Xaa-Xaa-Pro tripeptidyl-peptidase.
|
| Alternative Name(s) |
|---|
| Prolyl tripeptidyl peptidase. |
| Prolyltripeptidyl amino peptidase. |
| Prolyltripeptidyl aminopeptidase. |
| PTP-A. |
| TPP. |
| 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 |
| Comment(s) |
|---|
- 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.
|
| Cross-references |
|---|
| BRENDA | 3.4.14.12 |
| EC2PDB | 3.4.14.12 |
| ExplorEnz | 3.4.14.12 |
| PRIAM enzyme-specific profiles | 3.4.14.12 |
| KEGG Ligand Database for Enzyme Nomenclature | 3.4.14.12 |
| IUBMB Enzyme Nomenclature | 3.4.14.12 |
| IntEnz | 3.4.14.12 |
| MEDLINE | Find literature relating to 3.4.14.12 |
| MetaCyc | 3.4.14.12 |
| Rhea expert-curated reactions | 3.4.14.12 |
| UniProtKB/Swiss-Prot |
|
View entry in original ENZYME format
View entry in raw text format (no links)
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.-.-.-