CATH Domain 3bi1A02

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.50	3-Layer(bba) Sandwich
	3.50.30	Glucose Oxidase; domain 1
	3.50.30.30

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	3BI1
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Drosophila
Primary Citation	Structural basis of interactions between human glutamate carboxypeptidase II and its substrate analogs Barinka, C., Hlouchova, K., Rovenska, M., Majer, P., Dauter, M., Hin, N., Ko, Y.S., Tsukamoto, T., Slusher, B.S., Konvalinka, J., Lubkowski, J. J.Mol.Biol.