ENZYME entry: EC 3.4.14.12
Accepted Name |
Xaa-Xaa-Pro tripeptidyl-peptidase.
|
Alternative Name(s) |
prolyltripeptidyl aminopeptidase. |
prolyltripeptidyl amino peptidase. |
prolyl tripeptidyl peptidase. |
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 |
|
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