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Synonyms
glutamate racemase, race2, race1, d-glutamate racemase, glutamic acid racemases,
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L-glutamate = D-glutamate
L-glutamate = D-glutamate
deprotonation/protonation mechanism for racemization in which the breaking of the carbon-hydrogen bond at C-2 is partially rate-determining
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L-glutamate = D-glutamate
initial step is the proton abstraction from the substrate alpha-carbon atom, which is mediated by an amino acid residue in the enzyme protein
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L-glutamate = D-glutamate
two base mechanism, removal of alpha-hydrogen is the rate determining step
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L-glutamate = D-glutamate
the enzyme uses a two-base mechanism in which two Cys thiolates serve as the general base/acid catalysts. An initial deprotonation event produces a resonance-stabilized carbanionic intermediate that is subsequently protonated on the opposite face to generate the enantiomeric product
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L-glutamate = D-glutamate
deprotonation/protonation mechanism. Two-base mechanism in which one enzymic base deprotonates the substrate, and the conjugate acid of a second enzymic base protonates the resulting intermediate from the opposite face
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L-glutamate = D-glutamate
the enzyme uses a two-base mechanism involving a deprotonation of the substrate at the alpha-position to form an anionic intermediate, followed by a reprotonation in the opposite stereochemical sense. Cys73 is responsible for the deprotonation of D-glutamate and Cys184 is responsible for the deprotonation of L-glutamate
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L-glutamate = D-glutamate
analysis of active site, mechanism
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L-glutamate = D-glutamate
molecular dynamics simulations, mechanism by which binding mismatches are propagated into an opening of the active site
L-glutamate = D-glutamate
glutamate racemase faces the difficult task of deprotonating a relatively low acidicity proton, the amino acids R-hydrogen, with a relatively poor base, a cysteine. The titration curves and the pK1/2 values of all of the ionizable residues for different structures leading from reactants to products are analyzed. From these results a concerted mechanism is proposed in which the Cys70 residue deprotonates the R-hydrogen of the substrate while, at the same time, being deprotonated by the Asp7 residue
L-glutamate = D-glutamate
the molecular mechanism involves deprotonation of the glutamate alpha-proton, followed by substrate reprotonation on the opposite stereochemical face
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L-glutamate = D-glutamate
MurI is a member of the two-base mechanism (dual-cysteine) racemase family, where two essential active-site cysteine residues act as catalytic base and acid to stereospecifically de- and reprotonate, respectively, the alpha position of glutamate in order to enact substrate racemization
L-glutamate = D-glutamate
MurI is a member of the two-base mechanism (dual-cysteine) racemase family, where two essential active-site cysteine residues act as catalytic base and acid to stereospecifically de- and reprotonate, respectively, the alpha position of glutamate in order to enact substrate racemization. C185 of BsMurI corresponds to the essential catalytic cysteine residue that deprotonates an incoming L-glutamate substrate (or reprotonates a carbanionic intermediate to form the D-stereoconfiguration)
L-glutamate = D-glutamate
MurI is a member of the two-base mechanism (dual-cysteine) racemase family, where two essential active-site cysteine residues act as catalytic base and acid to stereospecifically de- and reprotonate, respectively, the alpha position of glutamate in order to enact substrate racemization. C185 of BsMurI corresponds to the essential catalytic cysteine residue that deprotonates an incoming L-glutamate substrate (or reprotonates a carbanionic intermediate to form the D-stereoconfiguration)
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L-glutamate = D-glutamate
MurI is a member of the two-base mechanism (dual-cysteine) racemase family, where two essential active-site cysteine residues act as catalytic base and acid to stereospecifically de- and reprotonate, respectively, the alpha position of glutamate in order to enact substrate racemization
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L-glutamate = D-glutamate
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D-serine-O-sulfate
L-serine-O-sulfate
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r
L-2-aminoadipic acid
D-2-aminoadipic acid
L-Homocysteinesulfinate
D-Homocysteinesulfinate
additional information
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D-Glu
L-Glu
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D-Glu
L-Glu
Lactic acid bacteria
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D-glutamate
L-glutamate
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D-glutamate
L-glutamate
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D-glutamate
L-glutamate
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r
D-glutamate
L-glutamate
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catalytic action of glutamate racemase is driven by its own substrate, D-glutamate
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r
D-glutamate
L-glutamate
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r
D-glutamate
L-glutamate
enzyme catalyzes the formation of D-glutamate from L-glutamate through a 1,1-proton transfer mechanism which reversibly inverts the stereochemistry at the alpha-carbon of glutamate
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r
D-glutamate
L-glutamate
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D-glutamate
L-glutamate
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D-glutamate
L-glutamate
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r
D-glutamate
L-glutamate
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r
D-glutamate
L-glutamate
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r
D-glutamate
L-glutamate
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r
D-glutamate
L-glutamate
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r
D-glutamate
L-glutamate
D-Glu binding structure, overview
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r
D-glutamate
L-glutamate
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r
D-glutamate
L-glutamate
D-Glu binding structure, overview
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r
D-glutamate
L-glutamate
D-Glu binding structure, overview
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r
D-glutamate
L-glutamate
D-Glu binding structure, overview
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r
L-2-aminoadipic acid
D-2-aminoadipic acid
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L-2-aminoadipic acid
D-2-aminoadipic acid
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L-Glu
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glutamate racemase is mainly concerned in D-Glu synthesis for poly-gamma-glutamate production
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L-Glu
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glutamate racemase is mainly concerned in D-Glu synthesis for poly-gamma-glutamate production
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L-Glu
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the biosynthesis of D-Glu, one of the essential components of bacterial cell-wall peptidoglycan, is catalyzed by glutamate racemase
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L-Glu
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Lactic acid bacteria
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the biosynthesis of D-Glu, one of the essential components of bacterial cell-wall peptidoglycan, is catalyzed by glutamate racemase
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L-glutamate
D-glutamate
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L-glutamate
D-glutamate
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L-glutamate
D-glutamate
the enzyme is responsible for the synthesis of D-glutamate, an essential building block of the peptidoglycan layer in bacterial cell walls
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L-glutamate
D-glutamate
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L-glutamate
D-glutamate
Q81LA8, Q81UL8
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L-glutamate
D-glutamate
Q81LA8, Q81UL8
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L-glutamate
D-glutamate
Q81LA8, Q81UL8
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r
L-glutamate
D-glutamate
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L-glutamate
D-glutamate
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L-glutamate
D-glutamate
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L-glutamate
D-glutamate
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r
L-glutamate
D-glutamate
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L-glutamate
D-glutamate
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r
L-glutamate
D-glutamate
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r
L-glutamate
D-glutamate
enzyme catalyzes the formation of D-glutamate from L-glutamate through a 1,1-proton transfer mechanism which reversibly inverts the stereochemistry at the alpha-carbon of glutamate
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r
L-glutamate
D-glutamate
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r
L-glutamate
D-glutamate
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r
L-glutamate
D-glutamate
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r
L-glutamate
D-glutamate
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L-glutamate
D-glutamate
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MurI enzymes from the Gram-positive species Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium share similar biophysical and biochemical characteristics that are distinct from Escherichia coli and Helicobacter pylori MurI
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r
L-glutamate
D-glutamate
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MurI enzymes from the Gram-positive species Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium share similar biophysical and biochemical characteristics that are distinct from Escherichia coli and Helicobacter pylori MurI
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r
L-glutamate
D-glutamate
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L-glutamate
D-glutamate
enzyme catalyzes the formation of D-glutamate from L-glutamate through a 1,1-proton transfer mechanism which reversibly inverts the stereochemistry at the alpha-carbon of glutamate
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L-glutamate
D-glutamate
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L-glutamate
D-glutamate
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L-glutamate
D-glutamate
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L-glutamate
D-glutamate
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L-glutamate
D-glutamate
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L-glutamate
D-glutamate
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r
L-glutamate
D-glutamate
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L-glutamate
D-glutamate
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L-glutamate
D-glutamate
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the enzyme provides bacteria with a source of D-glutamate for use in peptidoglycan biosynthesis
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L-glutamate
D-glutamate
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L-glutamate
D-glutamate
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r
L-glutamate
D-glutamate
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r
L-glutamate
D-glutamate
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r
L-glutamate
D-glutamate
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r
L-glutamate
D-glutamate
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r
L-glutamate
D-glutamate
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L-glutamate
D-glutamate
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r
L-glutamate
D-glutamate
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r
L-glutamate
D-glutamate
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MurI enzymes from the Gram-positive species Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium share similar biophysical and biochemical characteristics that are distinct from Escherichia coli and Helicobacter pylori MurI
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L-glutamate
D-glutamate
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r
L-glutamate
D-glutamate
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r
L-glutamate
D-glutamate
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r
L-glutamate
D-glutamate
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L-glutamate
D-glutamate
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L-glutamate
D-glutamate
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L-glutamate
D-glutamate
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L-Homocysteinesulfinate
D-Homocysteinesulfinate
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L-Homocysteinesulfinate
D-Homocysteinesulfinate
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slightly serves as substrate
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additional information
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Chlamydia trachomatis dapF encodes a bifunctional enzyme capable of both D-glutamate racemase and diaminopimelate epimerase, EC 5.1.1.7, activities. Diaminopimelate and glutamate appear to be competitive substrates, indicating that they share an active site despite the racemase reaction requiring the PLP cofactor
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additional information
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the enzyme is an endogenous DNA gyrase inhibitor
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additional information
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enzyme does not catalyze the exchange between 2-oxolutarate and DL-Glu
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additional information
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enzyme does not catalyze the exchange between 2-oxolutarate and DL-Glu
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additional information
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the enzyme uses a two-base mechanism involving a deprotonation of the substrate at the alpha-position to form an anionic intermediate, followed by a reprotonation in the opposite stereochemical sense. Cys73 is responsible for the deprotonation of D-glutamate and Cys184 is responsible for the deprotonation of L-glutamate
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additional information
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enzyme exhibits both racemization activity and DNA gyrase inhibition. The two activities are unlinked and independent of each other. Enzyme-DNA gyrase interaction influences gyrase activity but has no effect on the racemization activity
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additional information
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in addition to racemization activity, enzyme exhibits DNA gyrase activity by preventing DNA binding of gyrase. Sequestration of gyrase results in inhibition of all reactions catalyzed by DNA gyrase. Overexpression additiionally provides protection against ciprofloxacin
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additional information
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in addition to racemization activity, enzyme exhibits DNA gyrase activity by preventing DNA binding of gyrase. Sequestration of gyrase results in inhibition of all reactions catalyzed by DNA gyrase. Overexpression additionally provides protection against ciprofloxacin
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additional information
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the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria
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additional information
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the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria
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additional information
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the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria
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additional information
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the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria
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additional information
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the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria
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additional information
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the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria
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5.1.1.3 glutamate racemase
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