EC |
3.4.19.3 |
Accepted name: |
pyroglutamyl-peptidase I |
Reaction: |
Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro |
Other name(s): |
5-oxoprolyl-peptidase; pyrase; pyroglutamate aminopeptidase; pyroglutamyl aminopeptidase; L-pyroglutamyl peptide hydrolase; pyrrolidone-carboxyl peptidase; pyrrolidone-carboxylate peptidase; pyrrolidonyl peptidase; L-pyrrolidonecarboxylate peptidase; pyroglutamidase; pyrrolidonecarboxylyl peptidase |
Comments: |
A cysteine peptidase, known from bacteria, plants and animals. The enzyme from bacterial sources is used in protein sequencing, and is the type example of peptidase family C15. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9075-21-2 |
References: |
1. |
Tsuru, D., Nakamura, K., Yoshimoto, T. and Fujiwara, K. Pyroglutamyl-peptidase from Bacillus amyloliquefaciens. An improved purification method and some properties of the enzyme. Biochim. Biophys. Acta 791 (1984) 117–122. |
2. |
Awadé, A.C., Cleuziat, P., Gonzalès, T. and Robert-Baudouy, J. Pyrrolidone carboxyl peptidase (Pcp): an enzyme that removes pyroglutamic acid (pGlu) from pGlu-peptides and pGlu-proteins. Proteins Struct. Funct. Genet. 20 (1994) 34–51. [DOI] [PMID: 7824521] |
3. |
Patti, J.M., Schneider, A., Garza, N. and Boles, J.O. Isolation and characterization of pcp, a gene encoding a pyrrolidone carboxyl peptidase in Staphylococcus aureus. Gene 166 (1995) 95–99. [DOI] [PMID: 8529900] |
4. |
Le Saux, O., Gonzalès, T. and Robert-Baudouy, J. Mutational analysis of the active site of Pseudomonas fluorescens pyrrolidone carboxyl peptidase. J. Bacteriol. 178 (1996) 3308–3313. [DOI] [PMID: 8655512] |
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[EC 3.4.19.3 created 1972 as EC 3.4.11.8, transferred 1981 to EC 3.4.19.3, modified 1997] |
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