| Pyroglutamyl-peptidase I | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.19.3 | ||||||||
| CAS no. | 9075-21-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Pyroglutamyl-peptidase I ( EC 3.4.19.3, also known as Pyrrolidonyl peptidase, is an enzyme (a cysteine peptidase) found in bacteria, plants and animals.
It can be used to distinguish certain Streptococcal organisms. [1]
Other names are 5-oxoprolyl-peptidase, pyrase, pyrrolidonyl arylamidase, pyroglutamate aminopeptidase, pyroglutamyl aminopeptidase, L-pyroglutamyl peptide hydrolase, pyrrolidone-carboxyl peptidase, pyrrolidone-carboxylate peptidase, pyrrolidonyl peptidase, L-pyrrolidonecarboxylate peptidase, pyroglutamidase, pyrrolidonecarboxylyl peptidase) is an enzyme. [2] [3] [4] [5] This enzyme catalyses the following chemical reaction
- Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro
- ^ Panosian KJ, Edberg SC (March 1989). "Measurement of constitutive L-pyrrolidonyl peptidase activity from Streptococcus and Enterococcus using tetrazotized 0-dianisidine". Antonie van Leeuwenhoek. 55 (3): 269–75. doi: 10.1007/BF00393855. PMID 2569292.
- ^ Tsuru D, Nakamura K, Yoshimoto T, Fujiwara K (1984). "Pyroglutamyl-peptidase from Bacillus amyloliquefaciens. An improved purification method and some properties of the enzyme". Biochim. Biophys. Acta. 791 (2): 117–122. doi: 10.1016/0167-4838(84)90001-3.
- ^ Awadé AC, Cleuziat P, Gonzalès T, Robert-Baudouy J (September 1994). "Pyrrolidone carboxyl peptidase (Pcp): an enzyme that removes pyroglutamic acid (pGlu) from pGlu-peptides and pGlu-proteins". Proteins. 20 (1): 34–51. doi: 10.1002/prot.340200106. PMID 7824521.
- ^ Patti JM, Schneider A, Garza N, Boles JO (December 1995). "Isolation and characterization of pcp, a gene encoding a pyrrolidone carboxyl peptidase in Staphylococcus aureus". Gene. 166 (1): 95–9. doi: 10.1016/0378-1119(95)00561-0. PMID 8529900.
- ^ Le Saux O, Gonzales T, Robert-Baudouy J (June 1996). "Mutational analysis of the active site of Pseudomonas fluorescens pyrrolidone carboxyl peptidase". Journal of Bacteriology. 178 (11): 3308–13. PMC 178084. PMID 8655512.
- Pyroglutamyl-peptidase+I at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| Pyroglutamyl-peptidase I | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.19.3 | ||||||||
| CAS no. | 9075-21-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Pyroglutamyl-peptidase I ( EC 3.4.19.3, also known as Pyrrolidonyl peptidase, is an enzyme (a cysteine peptidase) found in bacteria, plants and animals.
It can be used to distinguish certain Streptococcal organisms. [1]
Other names are 5-oxoprolyl-peptidase, pyrase, pyrrolidonyl arylamidase, pyroglutamate aminopeptidase, pyroglutamyl aminopeptidase, L-pyroglutamyl peptide hydrolase, pyrrolidone-carboxyl peptidase, pyrrolidone-carboxylate peptidase, pyrrolidonyl peptidase, L-pyrrolidonecarboxylate peptidase, pyroglutamidase, pyrrolidonecarboxylyl peptidase) is an enzyme. [2] [3] [4] [5] This enzyme catalyses the following chemical reaction
- Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro
- ^ Panosian KJ, Edberg SC (March 1989). "Measurement of constitutive L-pyrrolidonyl peptidase activity from Streptococcus and Enterococcus using tetrazotized 0-dianisidine". Antonie van Leeuwenhoek. 55 (3): 269–75. doi: 10.1007/BF00393855. PMID 2569292.
- ^ Tsuru D, Nakamura K, Yoshimoto T, Fujiwara K (1984). "Pyroglutamyl-peptidase from Bacillus amyloliquefaciens. An improved purification method and some properties of the enzyme". Biochim. Biophys. Acta. 791 (2): 117–122. doi: 10.1016/0167-4838(84)90001-3.
- ^ Awadé AC, Cleuziat P, Gonzalès T, Robert-Baudouy J (September 1994). "Pyrrolidone carboxyl peptidase (Pcp): an enzyme that removes pyroglutamic acid (pGlu) from pGlu-peptides and pGlu-proteins". Proteins. 20 (1): 34–51. doi: 10.1002/prot.340200106. PMID 7824521.
- ^ Patti JM, Schneider A, Garza N, Boles JO (December 1995). "Isolation and characterization of pcp, a gene encoding a pyrrolidone carboxyl peptidase in Staphylococcus aureus". Gene. 166 (1): 95–9. doi: 10.1016/0378-1119(95)00561-0. PMID 8529900.
- ^ Le Saux O, Gonzales T, Robert-Baudouy J (June 1996). "Mutational analysis of the active site of Pseudomonas fluorescens pyrrolidone carboxyl peptidase". Journal of Bacteriology. 178 (11): 3308–13. PMC 178084. PMID 8655512.
- Pyroglutamyl-peptidase+I at the U.S. National Library of Medicine Medical Subject Headings (MeSH)