CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.390 | Enolase-like; domain 1 |
|
3.30.390.10 | Enolase-like, N-terminal domain |
Domain Context
CATH Clusters
| Superfamily | Enolase-like, N-terminal domain |
| Functional Family | L-Ala-D/L-Glu epimerase |
Enzyme Information
| 5.1.1.20 |
L-Ala-D/L-Glu epimerase.
based on mapping to UniProt Q9WXM1
L-alanyl-D-glutamate = L-alanyl-L-glutamate.
-!- The enzyme, characterized from the bacteria Escherichia coli and Bacillus subtilis, is involved in the recycling of the murein peptide, of which L-Ala-D-Glu is a component. -!- In vitro the enzyme from E.coli epimerizes several L-Ala-L-X dipeptides with broader specificity than the enzyme from B.subtilis. -!- Formerly EC 5.1.1.n1.
|
UniProtKB Entries (1)
| Q9WXM1 |
AEEP_THEMA
Thermotoga maritima MSB8
L-Ala-D/L-Glu epimerase
|
PDB Structure
| PDB | 3DEQ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Discovery of a dipeptide epimerase enzymatic function guided by homology modeling and virtual screening.
Structure
|
