5.1.1.3: glutamate racemase
This is an abbreviated version!
For detailed information about glutamate racemase, go to the full flat file.
Word Map on EC 5.1.1.3
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5.1.1.3
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peptidoglycan
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l-glutamate
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cofactor-independent
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drug development
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pediococcus
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poly-gamma-glutamate
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pyrophilus
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pentosaceus
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fermenti
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ciceri
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stereoinversion
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medicine
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synthesis
- 5.1.1.3
- peptidoglycan
- l-glutamate
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cofactor-independent
- drug development
- pediococcus
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poly-gamma-glutamate
- pyrophilus
- pentosaceus
- fermenti
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ciceri
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stereoinversion
- medicine
- synthesis
Reaction
Synonyms
AAR, BAS0806, BAS4379, BcGR, BsGR, BsRacE, CBL/ALR, cystathionine beta-lyase, D-glutamate racemase, DapF, FnGR, GBAA_0847, GBAA_4717, GLR, GluR, glutamate racemase, glutamic acid racemases, GRL, HpMurI, MetC, More, MurI, RACE, RacE1, RacE2, Racemase, glutamate, Rv1338, TmCBL, wMelCBL
ECTree
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Substrates Products
Substrates Products on EC 5.1.1.3 - glutamate racemase
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REACTION DIAGRAM
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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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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D-glutamate
L-glutamate
D-Glu binding structure, overview
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r
D-glutamate
L-glutamate
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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
Mycolicibacterium smegmatis ATCC 700084 / mc(2)155
D-Glu binding structure, overview
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L-2-aminoadipic acid
D-2-aminoadipic acid
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?
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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
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
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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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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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
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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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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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-Homocysteinesulfinate
D-Homocysteinesulfinate
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slightly serves as substrate
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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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