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| PROSITE documentation PDOC01036 |
Pyrrolidone-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.
Technical section:
PROSITE methods (with tools and information) covered by this documentation:
| PYRASE_CYS, PS01334; Pyrrolidone-carboxylate peptidase cysteine active site (PATTERN) |
| Consensus pattern: |
[LIVF]-x-[GSAVC]-x-[LIVM]-S-x-[STAD]-A-G-x-[FY]-[LIVN]-C-[DNS]
C is the active site residue |
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE. |
|
|
|
| Matching PDB structures:
1A2Z 1AUG 1IOF 1IU8 ... [ALL] |
| PYRASE_GLU, PS01333; Pyrrolidone-carboxylate peptidase glutamic acid active site (PATTERN) |
| Consensus pattern: |
G-x(2)-[GAP]-x(4)-[LIV]-[ST]-x-E-[KR]-[LIVC]-[AG]-x-[NG]
E is the active site residue |
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE. |
|
|
|
| Matching PDB structures:
1A2Z 1AUG 1IOF 1IOI ... [ALL] |
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 |
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