This cell-surface-associated serine exopeptidase is found in the Gram-negative, anaerobic bacterium?Porphyromonas gingivalis, which has been implicated in adult periodontal disease [1]. 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 [1]. The size of the peptide does not affect the rate of reaction [1].
Cofactor
History
Reactions
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.
