The Enzyme Database

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Accepted name: Xaa-Xaa-Pro tripeptidyl-peptidase
Reaction: 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
Other name(s): prolyltripeptidyl amino peptidase; prolyl tripeptidyl peptidase; prolyltripeptidyl aminopeptidase; PTP-A; TPP
Comments: 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 the N-terminal tripeptide of peptides, such as interleukin-6. It has 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].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
1.  Banbula, A., Mak, P., Bugno, M., Silberring, J., Dubin, A., Nelson, D., Travis, J. and Potempa, J. Prolyl tripeptidyl peptidase from Porphyromonas gingivalis. A novel enzyme with possible pathological implications for the development of periodontitis. J. Biol. Chem. 274 (1999) 9246–9252. [DOI] [PMID: 10092598]
2.  Fujimura, S., Ueda, O., Shibata, Y. and Hirai, K. Isolation and properties of a tripeptidyl peptidase from a periodontal pathogen Prevotella nigrescens. FEMS Microbiol. Lett. 219 (2003) 305–309. [DOI] [PMID: 12620636]
[EC created 2006]

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