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.
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UniProtKB Entries (1)
P51981 |
AEEP_ECOLI
Escherichia coli K-12
L-Ala-D/L-Glu epimerase
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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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