Pyroglutamyl-peptidase I

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
Pyroglutamyl-peptidase I
Identifiers
EC number3.4.19.3
CAS number9075-21-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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

Human gene

PGPEP1

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 (2): 117–122. doi:10.1016/0167-4838(84)90001-3.
  2. 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.
  3. 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.
  4. 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.
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