Pyroglutamyl-peptidase I

Pyroglutamyl-peptidase I
Identifiers
EC number 3.4.19.3
CAS number 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, 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) is an enzyme.[1][2][3][4] 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

This cysteine peptidase is isolated from bacteria, plants and animals.

References

  1. 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: 117–122. doi:10.1016/0167-4838(84)90001-3.
  2. Awadé, A.C.; Cleuziat, P.; Gonzalès, T.; Robert-Baudouy, J. (1994). "Pyrrolidone carboxyl peptidase (Pcp): an enzyme that removes pyroglutamic acid (pGlu) from pGlu-peptides and pGlu-proteins". Proteins: Struct. Funct. Genet. 20: 34–51. doi:10.1002/prot.340200106. PMID 7824521.
  3. Patti, J.M.; Schneider, A.; Garza, N.; Boles, J.O. (1995). "Isolation and characterization of pcp, a gene encoding a pyrrolidone carboxyl peptidase in Staphylococcus aureus'". Gene. 166: 95–99. doi:10.1016/0378-1119(95)00561-0. PMID 8529900.
  4. Le Saux, O.; Gonzalès, T.; Robert-Baudouy, J. (1996). "Mutational analysis of the active site of Pseudomonas fluorescens pyrrolidone carboxyl peptidase". J. Bacteriol. 178: 3308–3313. PMID 8655512.
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