|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Protein-Reactions|
EC Number: 188.8.131.52
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
Mass balance status: Balance undetermined; a substrate lacks a chemical formula
Enzyme Commission Primary Name: Xaa-Xaa-Pro tripeptidyl-peptidase
Enzyme Commission Synonyms: prolyltripeptidyl amino peptidase, prolyl tripeptidyl peptidase, prolyltripeptidyl aminopeptidase, PTP-A, TPP
Taxonomic Range: Bacteria
Enzyme Commission Summary:
This reaction is defined as the hydrolysis of peptides with a proline residue at the third position (position P1) releasing the N-terminal tripeptide, where the amino acids in the fourth position 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.
Banbula99: Banbula A, Mak P, Bugno M, Silberring J, Dubin A, Nelson D, Travis J, Potempa J (1999). "Prolyl tripeptidyl peptidase from Porphyromonas gingivalis. A novel enzyme with possible pathological implications for the development of periodontitis." J Biol Chem 274(14);9246-52. PMID: 10092598
Fujimura03: Fujimura S, Ueda O, Shibata Y, Hirai K (2003). "Isolation and properties of a tripeptidyl peptidase from a periodontal pathogen Prevotella nigrescens." FEMS Microbiol Lett 219(2);305-9. PMID: 12620636
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