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
-
cofactor-independent
- drug development
- pediococcus
-
poly-gamma-glutamate
- pyrophilus
- pentosaceus
- fermenti
-
ciceri
-
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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KM Value
KM Value on EC 5.1.1.3 - glutamate racemase
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26
L-2-aminoadipic acid
His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
4.2
D-Glu
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in presence of 0.0065 mM of the activator UDP-N-acetylmuramyl-L-Ala
0.07
D-glutamate
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recombinant wild type enzyme, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/mL diaphorase, and 0.05 mM D-glutamate
0.1
D-glutamate
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mutant Q86A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.13
D-glutamate
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mutant Y221A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.14
D-glutamate
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mutant R25A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.16
D-glutamate
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mutant R214A/K106A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.17
D-glutamate
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mutant P99A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.25
D-glutamate
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mutant K29A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.25
D-glutamate
wild type enzyme, at 25 °C in 50 mM Tris-HCl (pH 8.0), 5 mM NAD+, 0.5 mM iodonitrotetrazolium chloride, 2.5 mM ADP, 20 units of L-glutamate dehydrogenase, 2 units of diaphorase and D-glutamate
0.3
D-glutamate
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mutant R214A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.42
D-glutamate
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mutant K106A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
1.5
D-glutamate
His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
1.7
D-glutamate
His-tagged recombinant BsGR, in potassium phosphate buffer (10 mM, pH 8.0)
1.7
D-glutamate
recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
8.6
D-glutamate
mutant T76A, at 25 °C in 50 mM Tris-HCl, pH 8.0, 5 mM NAD+, 0.5 mM iodonitrotetrazolium chloride, 2.5 mM ADP, 20 units of L-glutamate dehydrogenase, 2 units of diaphorase and D-glutamate
10
D-glutamate
His-tagged recombinant BsGR mutant V149A, in potassium phosphate buffer (10 mM, pH 8.0)
0.25
wild-type enzyme, pH and temperature not specified in the publication
0.26
L-glutamate
recombinant His-tagged enzyme, pH 8.0, 37°C, bicine buffer
0.74
L-glutamate
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demonstrates a high degree of asymmetry in substrate processing with the Michaelis constant for D-glutamate approximately tenfold lower than for L-glutamate
0.9
L-glutamate
His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
1.04
L-glutamate
recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
1.4
L-glutamate
recombinant His-tagged enzyme, pH 8.0, 70°C, bicine buffer
4.1
L-glutamate
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mutant P99A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
5.8
L-glutamate
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mutant R25A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
6.1
L-glutamate
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recombinant RacE2 wild type enzyme, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
7.2
L-glutamate
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mutant K29A, in 10 mM potassium phosphate (pH 8.2)and 0.2 mM dithiothreitol
8.8
L-glutamate
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mutant Q86A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
9.9
L-glutamate
-
mutant Y221A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
10.1
L-glutamate
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mutant R214A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
10.8
L-glutamate
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mutant K106A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
11
L-glutamate
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mutant R214A/K106A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
14
L-glutamate
His-tagged recombinant BsGR, in potassium phosphate buffer (10 mM, pH 8.0)
14
L-glutamate
wild type enzyme, 50 mM boric acid, 100 mM KCl, 0.2 mM dithiothreitol, pH 8.0 at 25°C in the presence of 0.22 microM glutamate racemase
47
L-glutamate
His-tagged recombinant BsGR mutant V149A, in potassium phosphate buffer (10 mM, pH 8.0)
additional information
additional information
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mutant V149A has a Km value for L-glutamate similar to that of RacE2 (4.6 mM versus 3.7 mM). In the reverse reaction, the Km of V149A for D-glutamate is the same as that of RacE2 (0.2 mM)
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additional information
additional information
Michaelis-Menten steady-state kinetics
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additional information
additional information
Michaelis-Menten steady-state kinetics
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additional information
additional information
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recombinant enzyme, steady state kinetic analysis
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