Pyroglutamyl-peptidase I

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Pyroglutamyl-peptidase I
Identifiers
EC no.3.4.19.3
CAS no.9075-21-2
Databases
IntEnzIntEnz view
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ExPASyNiceZyme view
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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 (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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