PROSITE documentation PDOC01036Pyrrolidone-carboxylate peptidase active sites
Description
Pyrrolidone-carboxylate peptidase (EC 3.4.19.3) (PYRase) (also known as pyroglutamyl peptidase) is the enzyme that selectively removes pyroglutamate (pGlu) from the N-terminus of proteins and peptides.
In bacteria and archebacteria PYRase (gene pcp) is a protein of 22-25 kD. It is a cysteine protease with a Cys-His-Glu catalytic triad [1,2]. We developed two signature patterns that respectively include the glutamate and cysteine active site residues.
Note:These proteins belong to family C15 in the classification of peptidases [3,E1].
Last update:December 2004 / Pattern and text revised.
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Technical section
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References
| 1 | Authors | Singleton M.R. Isupov M. Littlechild J. |
| Title | X-ray structure of pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis. | |
| Source | Structure 7:237-244(1999). | |
| PubMed ID | 10368293 |
| 2 | Authors | Odagaki Y. Hayashi A. Okada K. Hirotsu K. Kabashima T. Ito K. Yoshimoto T. Tsuru D. Sato M. Clardy J. |
| Title | The crystal structure of pyroglutamyl peptidase I from Bacillus amyloliquefaciens reveals a new structure for a cysteine protease. | |
| Source | Structure 7:399-411(1999). | |
| PubMed ID | 10196127 |
| 3 | Authors | Rawlings N.D. Barrett A.J. |
| Title | Families of cysteine peptidases. | |
| Source | Methods Enzymol. 244:461-486(1994). | |
| PubMed ID | 7845226 |
| E1 | Title | https://www.uniprot.org/docs/peptidas |
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