The Enzyme Database

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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. [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. [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. [PMID: 8655512]
[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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