Literature summary for 5.1.1.20 extracted from

Schmidt, D.M.; Hubbard, B.K.; Gerlt, J.A.
Evolution of enzymatic activities in the enolase superfamily: functional assignment of unknown proteins in Bacillus subtilis and Escherichia coli as L-Ala-D/L-Glu epimerases (2001), Biochemistry, 40, 15707-15715.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Bacillus subtilis
-	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
0.028	-	L-Ala-D-Asp	pH 8.5, 37°C	Bacillus subtilis
0.13	-	L-Ala-D-Glu	pH 8.5, 37°C	Escherichia coli
0.19	-	L-Ala-D-Asp	pH 8.5, 37°C	Escherichia coli
0.32	-	L-Ala-D-Glu	pH 8.5, 37°C	Bacillus subtilis
0.51	-	L-Ala-D-Met	pH 8.5, 37°C	Bacillus subtilis
0.69	-	L-Ala-D-Met	pH 8.5, 37°C	Escherichia coli
1.8	-	L-Ala-D-Gln	pH 8.5, 37°C	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
34955	-	x * 34955, calculated from sequence	Escherichia coli
34994	-	x * 34994, electrospray ionization mass spectrometry	Escherichia coli
39472	-	x * 39472, calculated from sequence	Bacillus subtilis
39500	-	x * 39500, electrospray ionization mass spectrometry	Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-Ala-D-Glu	Bacillus subtilis	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	L-Ala-L-Glu	-	r

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	O34508	-	-
Escherichia coli	P51981	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Bacillus subtilis
-	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
Gly-L-Glu	-	Escherichia coli	Gly-D-Glu	-	r
L-Ala-D-Asp	-	Bacillus subtilis	L-Ala-L-Asp	-	r
L-Ala-D-Asp	-	Escherichia coli	L-Ala-L-Asp	-	r
L-Ala-D-Gln	-	Escherichia coli	L-Ala-L-Gln	-	r
L-Ala-D-Glu	-	Bacillus subtilis	L-Ala-L-Glu	-	r
L-Ala-D-Glu	-	Escherichia coli	L-Ala-L-Glu	-	r
L-Ala-D-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	Bacillus subtilis	L-Ala-L-Glu	-	r
L-Ala-D-Met	-	Bacillus subtilis	L-Ala-L-Met	-	r
L-Ala-D-Met	-	Escherichia coli	L-Ala-L-Met	-	r
L-Ala-L-Ala	-	Escherichia coli	L-Ala-D-Ala	-	r
L-Ala-L-Asn	-	Escherichia coli	L-Ala-D-Asn	-	r
L-Ala-L-Asp	-	Bacillus subtilis	L-Ala-D-Asp	-	r
L-Ala-L-Asp	-	Escherichia coli	L-Ala-D-Asp	-	r
L-Ala-L-Gln	-	Escherichia coli	L-Ala-D-Gln	-	r
L-Ala-L-Glu	-	Bacillus subtilis	L-Ala-D-Glu	-	r
L-Ala-L-Glu	-	Escherichia coli	L-Ala-D-Glu	-	r
L-Ala-L-His	L-Ala-L-His is epimerized by YcjG at pH 8 but not at pH 6	Escherichia coli	L-Ala-D-His	-	r
L-Ala-L-Ile	-	Escherichia coli	L-Ala-D-Ile	-	r
L-Ala-L-Leu	-	Bacillus subtilis	L-Ala-D-Leu	-	r
L-Ala-L-Leu	-	Escherichia coli	L-Ala-D-Leu	-	r
L-Ala-L-Met	-	Bacillus subtilis	L-Ala-D-Met	-	r
L-Ala-L-Met	-	Escherichia coli	L-Ala-D-Met	-	r
L-Ala-L-Phe	-	Escherichia coli	L-Ala-D-Phe	-	r
L-Ala-L-Ser	-	Bacillus subtilis	L-Ala-D-Ser	-	r
L-Ala-L-Ser	-	Escherichia coli	L-Ala-D-Ser	-	r
L-Ala-L-Thr	-	Escherichia coli	L-Ala-D-Thr	-	r
L-Ala-L-Trp	-	Escherichia coli	L-Ala-D-Trp	-	r
L-Ala-L-Tyr	-	Escherichia coli	L-Ala-D-Tyr	-	r
L-Ala-L-Val	-	Escherichia coli	L-Ala-D-Val	-	r
L-Phe-L-Glu	-	Escherichia coli	L-Phe-D-Glu	-	r
L-Pro-L-Glu	-	Bacillus subtilis	L-Pro-D-Glu	-	r
L-Ser-L-Glu	-	Bacillus subtilis	L-Ser-D-Glu	-	r
L-Ser-L-Glu	-	Escherichia coli	L-Ser-D-Glu	-	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	Bacillus subtilis	?	-	?
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	Escherichia coli	?	-	?

Subunits

Subunits	Comment	Organism
?	x * 34955, calculated from sequence	Escherichia coli
?	x * 34994, electrospray ionization mass spectrometry	Escherichia coli
?	x * 39472, calculated from sequence	Bacillus subtilis
?	x * 39500, electrospray ionization mass spectrometry	Bacillus subtilis

Synonyms

Synonyms	Comment	Organism
AEE	-	Bacillus subtilis
YcjG	-	Escherichia coli
YkfB	-	Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Bacillus subtilis
37	-	assay at	Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism
0.053	-	L-Ala-D-Asp	pH 8.5, 37°C	Bacillus subtilis
1.1	-	L-Ala-D-Met	pH 8.5, 37°C	Bacillus subtilis
1.9	-	L-Ala-D-Met	pH 8.5, 37°C	Escherichia coli
3.3	-	L-Ala-D-Gln	pH 8.5, 37°C	Escherichia coli
10	-	L-Ala-D-Glu	pH 8.5, 37°C	Escherichia coli
15	-	L-Ala-D-Glu	pH 8.5, 37°C	Bacillus subtilis
17	-	L-Ala-D-Asp	pH 8.5, 37°C	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8.5	-	assay at	Bacillus subtilis
8.5	-	assay at	Escherichia coli

General Information

General Information	Comment	Organism
physiological function	the enzyme is involved in the recycling of the murein peptide, of which L-Ala-D-Glu is a component	Bacillus subtilis
physiological function	the enzyme is involved in the recycling of the murein peptide, of which L-Ala-D-Glu is a component	Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism
1.8	-	L-Ala-D-Gln	pH 8.5, 37°C	Escherichia coli
1.9	-	L-Ala-D-Asp	pH 8.5, 37°C	Bacillus subtilis
2.2	-	L-Ala-D-Met	pH 8.5, 37°C	Bacillus subtilis
2.8	-	L-Ala-D-Met	pH 8.5, 37°C	Escherichia coli
47	-	L-Ala-D-Glu	pH 8.5, 37°C	Bacillus subtilis
77	-	L-Ala-D-Glu	pH 8.5, 37°C	Escherichia coli
89	-	L-Ala-D-Asp	pH 8.5, 37°C	Escherichia coli