CATH Domain 5d29A03

CATH Classification

Level	CATH Code	Description
	1	Mainly Alpha
	1.20	Up-down Bundle
	1.20.930	Transcription Elongation Factor S-II; Chain A
	1.20.930.40	Transferrin receptor-like, dimerisation domain

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	5D29
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Unprecedented Binding Mode of Hydroxamate-Based Inhibitors of Glutamate Carboxypeptidase II: Structural Characterization and Biological Activity. Novakova, Z., Wozniak, K., Jancarik, A., Rais, R., Wu, Y., Pavlicek, J., Ferraris, D., Havlinova, B., Ptacek, J., Vavra, J., Hin, N., Rojas, C., Majer, P., Slusher, B.S., Tsukamoto, T., Barinka, C. J.Med.Chem.