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 | 3IWW |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Bioisosterism of urea-based GCPII inhibitors: Synthesis and structure-activity relationship studies.
Bioorg.Med.Chem.Lett.
|
