CATH Classification

Domain Context

CATH Clusters

Superfamily Transferrin receptor-like, dimerisation domain
Functional Family

Enzyme Information
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 and EC -!- Belongs to peptidase family M28. -!- Formerly EC

UniProtKB Entries (1)

Homo sapiens
Glutamate carboxypeptidase 2

PDB Structure

PDB 5F09
External Links
Primary Citation
Comparison of human glutamate carboxypeptidases II and III reveals their divergent substrate specificities.
Navratil, M., Tykvart, J., Schimer, J., Pachl, P., Navratil, V., Rokob, T.A., Hlouchova, K., Rulisek, L., Konvalinka, J.
Febs J.