CATH Domain 3d7dA01

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.40	3-Layer(aba) Sandwich
	3.40.630	Aminopeptidase
	3.40.630.10	Zn peptidases

Domain Context

CATH Clusters

Superfamily	Zn peptidases
Functional Family	Glutamate carboxypeptidase 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	3D7D
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Interactions between Human Glutamate Carboxypeptidase II and Urea-Based Inhibitors: Structural Characterization Barinka, C., Byun, Y., Dusich, C.L., Banerjee, S.R., Chen, Y., Castanares, M., Kozikowski, A.P., Mease, R.C., Pomper, M.G., Lubkowski, J. J.Med.Chem.