Xaa-Pro dipeptidyl-peptidase
| Xaa-Pro dipeptidyl-peptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.14.11 | ||||||||
| CAS number | 54249-88-6 | ||||||||
| 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-Pro dipeptidyl-peptidase (EC 3.4.14.11, X-prolyl dipeptidyl aminopeptidase, PepX, X-prolyl dipeptidyl peptidase is an enzyme.[1][2][3][4][5] It catalyses the following chemical reaction
- Hydrolyses Xaa-Pro bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Pro-p-nitroanilide and (sequentially) Tyr-Pro--Phe-Pro--Gly-Pro--Ile
The intracellular enzyme from Lactococcus lactis (190-kDa) is the type example of peptidase family S15.
References
- ↑ Zevaco, C.; Monnet, V.; Gripon, J.-C. (1990). "Intracellular X-prolyl dipeptidyl peptidase from Lactococcus lactis' spp. lactis: purification and properties". J. Appl. Bacteriol. 68: 357–366. doi:10.1111/j.1365-2672.1990.tb02886.x.
- ↑ Meyer-Barton, E.C.; Klein, J.R.; Imam, M.; Plapp, R. (1993). "Cloning and sequence analysis of the X-prolyl-dipeptidyl-aminopeptidase gene (pepX) from Lactobacillus delbrückii ssp. lactis DSM7290". Appl. Microbiol. Biotechnol. 40: 82–89. doi:10.1007/bf00170433. PMID 7765315.
- ↑ Habibi-Najafi, M.B.; Lee, B.H. (1994). "Purification and characterization of X-prolyl dipeptidyl peptidase from Lactobacillus casei' subsp. casei LLG". Appl. Microbiol. Biotechnol. 42: 280–286. doi:10.1007/s002530050250. PMID 7765768.
- ↑ Chich, J.-F.; Gripon, J.-C.; Ribadeau-Dumas, B. (1995). "Preparation of bacterial X-prolyl dipeptidyl aminopeptidase and its stabilization by organic cosolvents". Anal. Biochem. 224: 245–249. doi:10.1006/abio.1995.1036. PMID 7710078.
- ↑ Chich, J.-F.; Chapot-Chartier, M.P.; Ribadeau-Dumas, B.; Gripon, J.-C. (1995). "Identification of the active site serine of the X-prolyl aminopeptidase from Lactococcus lactis'". FEBS Lett. 314: 139–142. doi:10.1016/0014-5793(92)80960-o.
External links
- Xaa-Pro dipeptidyl-peptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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