KEGG   ENZYME: 3.4.14.12Help
Entry
EC 3.4.14.12                Enzyme                                 

Name
Xaa-Xaa-Pro tripeptidyl-peptidase;
prolyltripeptidyl amino peptidase;
prolyl tripeptidyl peptidase;
prolyltripeptidyl aminopeptidase;
PTP-A;
TPP
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Dipeptidyl-peptidases and tripeptidyl-peptidases
BRITE hierarchy
Reaction(IUBMB)
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
Comment
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].
History
EC 3.4.14.12 created 2006
Orthology
K18574  
Xaa-Xaa-Pro tripeptidyl-peptidase
Genes
PGI: 
PGN: 
PGT: 
Taxonomy
Reference
1  [PMID:10092598]
  Authors
Banbula A, Mak P, Bugno M, Silberring J, Dubin A, Nelson D, Travis J, Potempa J.
  Title
Prolyl tripeptidyl peptidase from Porphyromonas gingivalis. A novel enzyme with possible pathological implications for the development of periodontitis.
  Journal
J. Biol. Chem. 274 (1999) 9246-52.
  Sequence
[pgi:PG_1361]
Reference
2  [PMID:12620636]
  Authors
Fujimura S, Ueda O, Shibata Y, Hirai K.
  Title
Isolation and properties of a tripeptidyl peptidase from a periodontal pathogen Prevotella nigrescens.
  Journal
FEMS. Microbiol. Lett. 219 (2003) 305-9.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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