CATH Classification

Domain Context

CATH Clusters

Superfamily Prolyl oligopeptidase, N-terminal domain
Functional Family Prolyl endopeptidase

Enzyme Information

3.4.21.26
Prolyl oligopeptidase.
based on mapping to UniProt P23687
Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.
-!- Found in vertebrates, plants and Flavobacterium. -!- Generally cytosolic, commonly activated by thiol compounds. -!- Belongs to peptidase family S9A. -!- Formerly EC 3.4.22.18.

UniProtKB Entries (1)

P23687
PPCE_PIG
Sus scrofa
Prolyl endopeptidase

PDB Structure

PDB 4AMZ
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Molecular Dynamics, Crystallography and Mutagenesis Studies on the Substrate Gating Mechanism of Prolyl Oligopeptidase.
Kaszuba, K., Rog, T., Danne, R., Canning, P., Fulop, V., Juhasz, T., Szeltner, Z., St-Pierre, J.F., Garcia-Horsman, A., Mannisto, P.T., Karttunen, M., Hokkanen, J., Bunker, A.
Biochimie