| Xaa-Pro dipeptidyl-peptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.14.11 | ||||||||
| CAS no. | 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.
- ^ Zevaco C, Monnet V, Gripon JC (1990). "Intracellular X-prolyl dipeptidyl peptidase from Lactococcus lactis spp. lactis: purification and properties". Journal of Applied Bacteriology. 68 (4): 357–366. doi: 10.1111/j.1365-2672.1990.tb02886.x.
- ^ Meyer-Barton EC, Klein JR, Imam M, Plapp R (October 1993). "Cloning and sequence analysis of the X-prolyl-dipeptidyl-aminopeptidase gene (pepX) from Lactobacillus delbrückii ssp. lactis DSM7290". Applied Microbiology and Biotechnology. 40 (1): 82–9. doi: 10.1007/bf00170433. PMID 7765315.
- ^ Habibi-Najafi MB, Lee BH (1994). "Purification and characterization of X-prolyl dipeptidyl peptidase from Lactobacillus casei subsp. casei LLG". Appl. Microbiol. Biotechnol. 42 (2–3): 280–286. doi: 10.1007/s002530050250. PMID 7765768.
- ^ Chich JF, Gripon JC, Ribadeau-Dumas B (January 1995). "Preparation of bacterial X-prolyl dipeptidyl aminopeptidase and its stabilization by organic cosolvents". Analytical Biochemistry. 224 (1): 245–9. doi: 10.1006/abio.1995.1036. PMID 7710078.
- ^ Chich JF, Chapot-Chartier MP, Ribadeau-Dumas B, Gripon JC (December 1992). "Identification of the active site serine of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis". FEBS Letters. 314 (2): 139–42. doi: 10.1016/0014-5793(92)80960-o. PMID 1459244.
- Xaa-Pro+dipeptidyl-peptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| Xaa-Pro dipeptidyl-peptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.14.11 | ||||||||
| CAS no. | 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.
- ^ Zevaco C, Monnet V, Gripon JC (1990). "Intracellular X-prolyl dipeptidyl peptidase from Lactococcus lactis spp. lactis: purification and properties". Journal of Applied Bacteriology. 68 (4): 357–366. doi: 10.1111/j.1365-2672.1990.tb02886.x.
- ^ Meyer-Barton EC, Klein JR, Imam M, Plapp R (October 1993). "Cloning and sequence analysis of the X-prolyl-dipeptidyl-aminopeptidase gene (pepX) from Lactobacillus delbrückii ssp. lactis DSM7290". Applied Microbiology and Biotechnology. 40 (1): 82–9. doi: 10.1007/bf00170433. PMID 7765315.
- ^ Habibi-Najafi MB, Lee BH (1994). "Purification and characterization of X-prolyl dipeptidyl peptidase from Lactobacillus casei subsp. casei LLG". Appl. Microbiol. Biotechnol. 42 (2–3): 280–286. doi: 10.1007/s002530050250. PMID 7765768.
- ^ Chich JF, Gripon JC, Ribadeau-Dumas B (January 1995). "Preparation of bacterial X-prolyl dipeptidyl aminopeptidase and its stabilization by organic cosolvents". Analytical Biochemistry. 224 (1): 245–9. doi: 10.1006/abio.1995.1036. PMID 7710078.
- ^ Chich JF, Chapot-Chartier MP, Ribadeau-Dumas B, Gripon JC (December 1992). "Identification of the active site serine of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis". FEBS Letters. 314 (2): 139–42. doi: 10.1016/0014-5793(92)80960-o. PMID 1459244.
- Xaa-Pro+dipeptidyl-peptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)