Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 3.4.14.12

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Macromolecule Reactions Protein-Reactions

EC Number: 3.4.14.12

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: 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

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:3.4.14.12 , ENZYME:EC:3.4.14.12 , IUBMB-ExplorEnz:EC:3.4.14.12


References

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Wed Dec 17, 2014, biocyc12.