5.1.1.20: L-Ala-D/L-Glu epimerase
This is an abbreviated version!
For detailed information about L-Ala-D/L-Glu epimerase, go to the full flat file.
Word Map on EC 5.1.1.20
Reaction
Synonyms
AE epimerase, AEE, L-Ala-D/L-Glu epimerase, YcjG, YfkA, YfkB, YkfB
ECTree
5.1.1.20 L-Ala-D/L-Glu epimeraseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 5.1.1.20 - L-Ala-D/L-Glu epimerase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-Ala-L-His
L-Ala-D-His
L-Ala-L-His is epimerized by YcjG at pH 8 but not at pH 6
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-
r
L-Ala-D-Glu
L-Ala-L-Glu
the enzyme is involved in the recycling of the murein peptide, of which L-Ala-D-Glu is a component. The murein hydrolases degrade peptidoglycan to the final dipeptide L-Ala-D-Glu. If L-Ala-D-Glu is epimerized to L-Ala-L-Glu, hydrolysis can occur with bacterial dipeptidases
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r
additional information
?
-
no activity with L-Ala-L-Arg, L-Ala-L-Lys, L-Ala-L-Pro, L-Glu-L-Glu, L-Lys-L-Glu, L-Pro-L-Glu, L-Lys-L-Ala, or D-Ala-D-Ala
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?
additional information
?
-
-
no activity with L-Ala-L-Arg, L-Ala-L-Lys, L-Ala-L-Pro, L-Glu-L-Glu, L-Lys-L-Glu, L-Pro-L-Glu, L-Lys-L-Ala, or D-Ala-D-Ala
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?
additional information
?
-
The kinetic parameters suggest that L-Ala-D/L-Glu is the intrinsic substrate for the enzyme
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?
additional information
?
-
epimerization of the L-Glu residue is confirmed by NMR and MS analysis. Analyzing substrate specificity with dipeptides composed of different amino acids, YkfB has a narrow substrate specificity against both N- and C-terminal substrates
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?
additional information
?
-
The kinetic parameters suggest that L-Ala-D/L-Glu is the intrinsic substrate for the enzyme
-
-
?
additional information
?
-
epimerization of the L-Glu residue is confirmed by NMR and MS analysis. Analyzing substrate specificity with dipeptides composed of different amino acids, YkfB has a narrow substrate specificity against both N- and C-terminal substrates
-
-
?
additional information
?
-
no activity with L-Ala-L-Arg, L-Ala-L-Lys, L-Ala-L-Pro, L-Glu-L-Glu, L-Lys-L-Glu, L-Pro-L-Glu, L-Lys-L-Ala, or D-Ala-D-Ala
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-
?
additional information
?
-
-
no activity with L-Ala-L-Arg, L-Ala-L-Lys, L-Ala-L-Pro, L-Glu-L-Glu, L-Lys-L-Glu, L-Pro-L-Glu, L-Lys-L-Ala, or D-Ala-D-Ala
-
-
?
additional information
?
-
The kinetic parameters suggest that L-Ala-D/L-Glu is the intrinsic substrate for the enzyme
-
-
?
additional information
?
-
epimerization of the L-Glu residue is confirmed by NMR and MS analysis. Analyzing substrate specificity with dipeptides composed of different amino acids, YcjG shows a broad substrate specificity against dipeptides with L-Ala at the N-terminus but narrow specificity against dipeptides with L-Glu at the C-terminus
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-
?
