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1
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0027164569
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The synthesis of DL-3,3-Difluoroglutamic acid from a 3-oxoprolinol derivative
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Selected recent examples
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(1993)
Tetrahedron Letters
, vol.34
, pp. 4917-4920
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-
Hart1
Coward2
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5
-
-
0027263160
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Purification, cloning, and cofactor independence of glutamate racemase from Lactobacillus
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(1993)
Biochemistry
, vol.32
, pp. 3981-3990
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-
Gallo1
Knowles2
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7
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-
0027155359
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Isotope effects and the identification of catalytic residues in the reaction catalyzed by glutamate racemase
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(1993)
Biochemistry
, vol.32
, pp. 3998-4006
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-
Tanner1
Gallo2
Knowles3
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11
-
-
0025284368
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2-(4-Amino-4-carboxybutyl)aziridine-2-carboxylic acid. A potent irreversible inhibitor of diaminopimelic acid epimerase. Spontaneous formation from .alpha.-(halomethyl)diaminopimelic acids
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(1990)
Journal of Medicinal Chemistry
, vol.33
, pp. 2157-2162
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-
Gerhart1
Higgins2
Tardif3
Ducep4
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14
-
-
0019871816
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Irreversible inhibition of glutamate decarboxylase by .alpha.-(fluoromethyl)glutamic acid
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This compound has also been prepared by an alternate route.
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(1981)
Biochemistry
, vol.20
, pp. 506-511
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-
Kuo1
Rando2
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15
-
-
84912951186
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-
2O were referenced to HOD at 4.65 ppm.To further [[Truncated]]
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-
-
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18
-
-
0023043179
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Energetics and mechanism of proline racemase
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For related enzymes see, and references therein
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(1986)
Biochemistry
, vol.25
, pp. 2572-2577
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-
Albery1
Knowles2
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19
-
-
0016791954
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Reaction mechanism and structure of the active site of proline racemase
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(1975)
Biochemistry
, vol.14
, pp. 4515-4522
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-
Rudnick1
Abeles2
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23
-
-
0021135333
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Purification and properties of diaminopimelic acid epimerase from Escherichia coli.
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(1984)
J Biol Chem
, vol.259
, pp. 8907-8914
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-
Wiseman1
Nichols2
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24
-
-
84912901267
-
-
2b for racemase activity was employed in all kinetics measurements.
-
-
-
-
25
-
-
84912917328
-
-
Inhibition studies. A 0.1 M stock solution of (±)4 in 1N KOH was prepared by heating a solution of (±)3 at 85°C for 1.5 hrs. This was diluted into triethanolamine-HCl, pH 8, along with an equivalent amount of 1N HCl (final pH 8, final conc. 2 mM) immediately before use. The inhibitor solution was added to enzyme samples in Trien-HCl, pH 8, containing 2mM dithiothreitol at 25°C and incubated for timed intervals. The reaction was stopped by diluting aliquots directly into cuvettes. One-half of the racemase activity was lost during a two minute incubation with 0.4 mM inhibitor. When the same incubation was carried out in the presence of 1 mM d,l-glutamate only 15% of the activity was lost.
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-
-
-
26
-
-
84912908629
-
-
Electrospray Mass Spectra. A 1 mg/mL sample of racemase in phosphate buffer, pH 7, containing 1 mM dithiothreitol was prepared. To one-half of this solution was added a solution of (±)4 in 1N KOH, and to the other half was added 1N KOH. The final pH of these was solutions was about 8. The solutions were incubated at 37°C for 30 min and then analyzed.Iodoacetate-treated samples were prepared as follows. A solution of racemase (100 μL, 6 mg/mL) in phosphate buffer, pH 7.6, containing 0.7 mM, d,l-glutamate and 0.25 mM dithiothreitol was prepared. To one half of this sample was added a solution of (±)4 (neutralized immediately before use) and to the other half was added water. The samples were incubated at 37°C for 45 min. To each of the samples was added 6 M guanidine hydrochloride in a phosphate buffer, pH 7.3, containing 1.0 mM sodium iodoacetate. The samples were incubated in the dark at 25°C for 75 min and quenched [[Truncated]]
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-
-
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27
-
-
84912921334
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-
2b The observed mass was 28,309±4 daltons. The discrepancy (14 daltons) is likely due to a sequencing error that missassigned a single amino acid residue.
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-
-
-
28
-
-
3042934967
-
Tissue sulfhydryl groups
-
16 occuring in the absence of added dithiothreitol. Treatment with 4 reduced this value to 0.5 thiol groups per enzyme, which is consistent with alkylation of one of the cysteines.
-
(1959)
Archives of Biochemistry and Biophysics
, vol.82
, pp. 70-77
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-
Ellman1
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29
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-
84912931645
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10b,c
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