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 | Hydrophobic dipeptide epimerase |
Enzyme Information
5.1.1.20 |
L-Ala-D/L-Glu epimerase.
based on mapping to UniProt Q8A861
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)
Q8A861 |
AEEP_BACTN
Bacteroides thetaiotaomicron VPI-5482
L-Ala-D/L-Glu epimerase
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PDB Structure
PDB | 3IJI |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Homology models guide discovery of diverse enzyme specificities among dipeptide epimerases in the enolase superfamily.
Proc.Natl.Acad.Sci.USA
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