This cell-surface-associated serine exopeptidase is found in the Gram-negative, anaerobic bacterium Porphyromonas gingivalis, which has been implicated in adult periodontal disease.
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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 enzyme releases tripeptides from the free amino terminus of peptides and small proteins, such as interleukin-6.,
The size of the peptide does not affect the rate of reaction.,
This cell-surface-associated serine exopeptidase is found in the Gram-negative, anaerobic bacterium Porphyromonas gingivalis, which has been implicated in adult periodontal disease.
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| uniprot:name |
PTP-A,
Prolyl tripeptidyl peptidase,
Prolyltripeptidyl amino peptidase,
Prolyltripeptidyl aminopeptidase,
TPP,
Xaa-Xaa-Pro tripeptidyl-peptidase
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| uniprot:activity |
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.
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