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.
a two-base reaction mechanism typical for enolase superfamily enzymes, Mg2+-assisted general base-catalyzed abstraction of the alpha-proton of a carboxylic acid and stabilization of an enolate anion intermediate, overview
a two-base reaction mechanism typical for enolase superfamily enzymes, Mg2+-assisted general base-catalyzed abstraction of the alpha-proton of a carboxylic acid and stabilization of an enolate anion intermediate, overview
a two-base reaction mechanism typical for enolase superfamily enzymes, Mg2+-assisted general base-catalyzed abstraction of the alpha-proton of a carboxylic acid and stabilization of an enolate anion intermediate, overview
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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.
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
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
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
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
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
the enzyme belongs to the enolase superfamily enzymes. The enzyme reaction shows the common enolase family reaction mechanism: Mg2+-assisted general base-catalyzed abstraction of the alpha-proton of a carboxylic acid and stabilization of an enolate anion intermediate. The fate of the intermediate is determined by the active site of each enzyme to produce the specific product
the enzyme belongs to the enolase superfamily enzymes. The enzyme reaction shows the common enolase family reaction mechanism: Mg2+-assisted general base-catalyzed abstraction of the alpha-proton of a carboxylic acid and stabilization of an enolate anion intermediate. The fate of the intermediate is determined by the active site of each enzyme to produce the specific product
the enzyme belongs to the enolase superfamily enzymes. The enzyme reaction shows the common enolase family reaction mechanism: Mg2+-assisted general base-catalyzed abstraction of the alpha-proton of a carboxylic acid and stabilization of an enolate anion intermediate. The fate of the intermediate is determined by the active site of each enzyme to produce the specific product
the enzyme structure comprises an N-terminal capping domain and a C-terminal (beta/alpha)7beta-barrel, and the active site is located in the barrel domain. The Mg2+ ion forms a bidentate interaction with the alpha-carbonyl group of the Glu of the substrate and the alpha-carbon center to be epimerized is located between two conserved lysine residues, K162 and K268 in YkfB
the enzyme structure comprises an N-terminal capping domain and a C-terminal (beta/alpha)7beta-barrel, and the active site is located in the barrel domain. The Mg2+ ion forms a bidentate interaction with the alpha-carbonyl group of the Glu of the substrate and the alpha-carbon center to be epimerized is located between two conserved lysine residues, K162 and K268 in YkfB
the enzyme structure comprises an N-terminal capping domain and a C-terminal (beta/alpha)7beta-barrel, and the active site is located in the barrel domain. The Mg2+ ion forms a bidentate interaction with the alpha-carbonyl group of the Glu of the substrate and the alpha-carbon center to be epimerized is located between two conserved lysine residues
the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
the mutant enzyme shows o-succinylbenzoate synthase activity at low level that is sufficient to permit anaerobic growth by an o-succinylbenzoate synthase-deficient strain of Escherichia coli, wild-type enzyme show
the mutation is located at the end of the eighth beta-strand of the (beta/alpha)8-barrel. The mutant enzyme has no detectable muconate lactonizing activity. The mutant enzyme catalyzes the o-succinylbenzoate synthase reaction
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
Gulick, A.M.; Schmidt, D.M.; Gerlt, J.A.; Rayment, I.
Evolution of enzymatic activities in the enolase superfamily: crystal structures of the L-Ala-D/L-Glu epimerases from Escherichia coli and Bacillus subtilis
Klenchin, V.A.; Schmidt, D.M.; Gerlt, J.A.; Rayment, I.
Evolution of enzymatic activities in the enolase superfamily: structure of a substrate-liganded complex of the L-Ala-D/L-Glu epimerase from Bacillus subtilis
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Enzyme Nomenclature
5.1.1.20 L-Ala-D/L-Glu epimerase
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