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ENZYME entry: EC 18.104.22.168
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|Prolyl tripeptidyl peptidase.|
|Prolyltripeptidyl amino peptidase.|
|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.
|PRIAM enzyme-specific profiles||22.214.171.124|
|KEGG Ligand Database for Enzyme Nomenclature||126.96.36.199|
|IUBMB Enzyme Nomenclature||188.8.131.52|
|MEDLINE||Find literature relating to 184.108.40.206|
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