Information on EC 5.1.1.20 - L-Ala-D/L-Glu epimerase

Word Map on EC 5.1.1.20
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.1.1.20
-
RECOMMENDED NAME
GeneOntology No.
L-Ala-D/L-Glu epimerase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-alanyl-D-glutamate = L-alanyl-L-glutamate
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
muropeptide degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
L-alanyl-D-glutamate epimerase
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 Escherichia coli epimerizes several L-Ala-L-X dipeptides with broader specificity than the enzyme from Bacillus subtilis.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Gly-L-Glu
Gly-D-Glu
show the reaction diagram
-
-
-
r
L-Ala-D-Asp
L-Ala-L-Asp
show the reaction diagram
L-Ala-D-Gln
L-Ala-L-Gln
show the reaction diagram
-
-
-
r
L-Ala-D-Glu
L-Ala-L-Glu
show the reaction diagram
L-Ala-D-Met
L-Ala-L-Met
show the reaction diagram
L-Ala-L-Ala
L-Ala-D-Ala
show the reaction diagram
-
-
-
r
L-Ala-L-Asn
L-Ala-D-Asn
show the reaction diagram
-
-
-
r
L-Ala-L-Asp
L-Ala-D-Asp
show the reaction diagram
L-Ala-L-Gln
L-Ala-D-Gln
show the reaction diagram
-
-
-
r
L-Ala-L-Glu
L-Ala-D-Glu
show the reaction diagram
L-Ala-L-His
L-Ala-D-His
show the reaction diagram
L-Ala-L-His is epimerized by YcjG at pH 8 but not at pH 6
-
-
r
L-Ala-L-Ile
L-Ala-D-Ile
show the reaction diagram
-
-
-
r
L-Ala-L-Leu
L-Ala-D-Leu
show the reaction diagram
L-Ala-L-Met
L-Ala-D-Met
show the reaction diagram
L-Ala-L-Phe
L-Ala-D-Phe
show the reaction diagram
-
-
-
r
L-Ala-L-Ser
L-Ala-D-Ser
show the reaction diagram
L-Ala-L-Thr
L-Ala-D-Thr
show the reaction diagram
-
-
-
r
L-Ala-L-Trp
L-Ala-D-Trp
show the reaction diagram
-
-
-
r
L-Ala-L-Tyr
L-Ala-D-Tyr
show the reaction diagram
-
-
-
r
L-Ala-L-Val
L-Ala-D-Val
show the reaction diagram
-
-
-
r
L-Phe-L-Glu
L-Phe-D-Glu
show the reaction diagram
-
-
-
r
L-Pro-L-Glu
L-Pro-D-Glu
show the reaction diagram
-
-
-
r
L-Ser-L-Glu
L-Ser-D-Glu
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-Ala-D-Glu
L-Ala-L-Glu
show the reaction diagram
O34508
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
-
-
r
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.028 - 0.19
L-Ala-D-Asp
1.8
L-Ala-D-Gln
-
pH 8.5, 37C
0.13 - 0.32
L-Ala-D-Glu
0.51 - 0.69
L-Ala-D-Met
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.053 - 17
L-Ala-D-Asp
3.3
L-Ala-D-Gln
Escherichia coli
-
pH 8.5, 37C
10 - 15
L-Ala-D-Glu
1.1 - 1.9
L-Ala-D-Met
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.9 - 89
L-Ala-D-Asp
197790
1.8
L-Ala-D-Gln
Escherichia coli
-
pH 8.5, 37C
197792
47 - 77
L-Ala-D-Glu
194908
2.2 - 2.8
L-Ala-D-Met
197791
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34955
-
x * 34955, calculated from sequence
34994
-
x * 34994, electrospray ionization mass spectrometry
39472
-
x * 39472, calculated from sequence
39500
-
x * 39500, electrospray ionization mass spectrometry
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals are grown by hanging drop methods at room temperature
-
structure of the complex of L-Ala-L-Glu with the enzyme
-
crystals are grown by hanging drop methods at room temperature
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I19A/D297G
-
the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
I19C/D297G
-
the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
I19F/D297G
-
the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
I19L/D297G
-
the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
I19N/D297G
-
the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
I19S/D297G
-
the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
I19T/D297G
-
the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
I19V/D297G
-
the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
I19W/D297G
-
the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
I19Y/D297G
-
the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor