MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateMacromolecule ReactionsProtein-Reactions

EC Number:

The direction shown, i.e. which substrates are on the left and right sides, 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.

Citations: [Fujimura03, Banbula99]

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:


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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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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