CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.20 | TIM Barrel |
|
3.20.20.120 | Enolase-like C-terminal domain |
Domain Context
CATH Clusters
| Superfamily | Enolase-like C-terminal domain |
| Functional Family | Dipeptide epimerase |
Enzyme Information
| 5.1.1.20 |
L-Ala-D/L-Glu epimerase.
based on mapping to UniProt P51981
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)
| P51981 |
AEEP_ECOLI
Escherichia coli K-12
L-Ala-D/L-Glu epimerase
|
PDB Structure
| PDB | 1JPD |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Evolution of enzymatic activities in the enolase superfamily: crystal structures of the L-Ala-D/L-Glu epimerases from Escherichia coli and Bacillus subtilis.
Biochemistry
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