Biology:Xaa-Xaa-Pro tripeptidyl-peptidase
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Short description: Class of enzymes
| Xaa-Xaa-Pro tripeptidyl-peptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.14.12 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Xaa-Xaa-Pro tripeptidyl-peptidase (EC 3.4.14.12, prolyltripeptidyl amino peptidase, prolyl tripeptidyl peptidase, prolyltripeptidyl aminopeptidase, PTP-A, TPP) is an enzyme.[1][2] It catalyses the following chemical 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
This cell-surface-associated serine exopeptidase is found in the Gram-negative, anaerobic bacterium Porphyromonas gingivalis.
References
- ↑ "Prolyl tripeptidyl peptidase from Porphyromonas gingivalis. A novel enzyme with possible pathological implications for the development of periodontitis". The Journal of Biological Chemistry 274 (14): 9246–52. April 1999. doi:10.1074/jbc.274.14.9246. PMID 10092598.
- ↑ "Isolation and properties of a tripeptidyl peptidase from a periodontal pathogen Prevotella nigrescens". FEMS Microbiology Letters 219 (2): 305–9. February 2003. doi:10.1016/s0378-1097(03)00048-x. PMID 12620636.
External links
- Xaa-Xaa-Pro+tripeptidyl-peptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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