CATH Classification

Domain Context

CATH Clusters

Superfamily Transferrin receptor-like, dimerisation domain
Functional Family

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 2OR4
External Links
Method X-RAY DIFFRACTION
Organism Drosophila
Primary Citation
Structural insight into the pharmacophore pocket of human glutamate carboxypeptidase II.
Barinka, C., Rovenska, M., Mlcochova, P., Hlouchova, K., Plechanovova, A., Majer, P., Tsukamoto, T., Slusher, B.S., Konvalinka, J., Lubkowski, J.
J.Med.Chem.