CATH Classification

Domain Context

CATH Clusters

Superfamily 3.50.30.30
Functional Family N-acetylated-alpha-linked acidic dipeptidase 2

Enzyme Information

3.4.17.21
Glutamate carboxypeptidase II.
based on mapping to UniProt Q04609
Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.
-!- Hydrolyzes alpha-peptide bonds in Ac-Asp-Glu, Asp-Glu, and Glu-Glu, but also gamma-glutamyl bonds in gamma-Glu-Glu and folylpoly-gamma- glutamates. -!- With folylpoly-gamma-glutamates, shows processive carboxypeptidase activity to produce pteroylmonoglutamate. -!- Does not hydrolyze Ac-beta-Asp-Glu. -!- Inhibited by quisqualic acid, Ac-beta-Asp-Glu, and 2-phosphonomethyl- pentanedioate. -!- The release of C-terminal glutamate from folylpoly-gamma-glutamates is also catalyzed by EC 3.4.17.11 and EC 3.4.19.9. -!- Belongs to peptidase family M28. -!- Formerly EC 3.4.19.8.

UniProtKB Entries (1)

Q04609
FOLH1_HUMAN
Homo sapiens
Glutamate carboxypeptidase 2

PDB Structure

PDB 4P4I
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Design of composite inhibitors targeting glutamate carboxypeptidase II: the importance of effector functionalities.
Novakova, Z., Cerny, J., Choy, C.J., Nedrow, J.R., Choi, J.K., Lubkowski, J., Berkman, C.E., Barinka, C.
Febs J.