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5.1.1.1: alanine racemase

This is an abbreviated version!
For detailed information about alanine racemase, go to the full flat file.

Word Map on EC 5.1.1.1

Reaction

L-alanine
=
D-alanine

Synonyms

1SFT, AAR, alanine racemase, AlaR, ALR, alr-2, ALR1, ALR2, Alr2 racemase, AlrA, AlrAba, AlrBax, AlrMtb, alrTt, ARL, BA0252, BAS0238, CBL/ALR, CdAlr, cystathionine beta-lyase, D-alanine racemase, DadB, DadX, dadXOF4, dal1, EcAlr, EcCBL, EfAlaR, L-Alanine racemase, L-Alanine:D-alanine racemase, MBalr1, MBAlr2, MetC, More, MurI, OEOE_1641, PDB, Racemase, alanine, tAlaRac, TmCBL, wMelCBL

ECTree

     5 Isomerases
         5.1 Racemases and epimerases
             5.1.1 Acting on amino acids and derivatives
                5.1.1.1 alanine racemase

Crystallization

Crystallization on EC 5.1.1.1 - alanine racemase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, hanging drop vapour diffusion method, mixing of 0.001 ml of 9 mg/ml protein in 25 mM Tris-HCl, pH 7.5, 15 mM NaCl, 10% v/v glycerol, 3 mM 2-mercaptoethanol, and 0.1 mM pyridoxal-5'-phosphate, with 0.001 ml of reservoir solution containing 2% v/v Tacsimate pH 5.0, 0.1 M sodium citrate tribasic dihydrate, pH 5.5, 16% w/v PEG 3350, equilibration against 1 ml of reservoir solution, method optimization, 2 days, X-ray diffraction structure determination and analysis at 2.3 A resolution
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purified recombinant enzyme, sitting drop vapour diffusion, 6 mg/ml protein solution is mixed with crystallization solution containing 100 mM MES, pH 6.0, 200 mM CaCl2, and 20% PEG 6000, 4 days, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement using the ligand- and water-free monomer structure of Pseudomonas aeruginosa as the search model
purified enzyme, hanging drop vapour diffusion, method, X-ray diffraction structure determination and analysis at 1.8 A resolution, molecular replacement method using the crystal structure of native alanine racemase from Bacillus stearothermophilus as search model, PDB ID 1SFT
Alkalihalophilus pseudofirmus
using the hanging-drop vapour diffusion method at 291 K
Alkalihalophilus pseudofirmus
enzyme is subjected to a reductive-methylation procedure
Q81VF6
using the vapor diffusion method with sitting drops
Q81VF6
purified recombinant enzyme, hanging drop vapour diffusion method, mixing of 12 mg/ml protein in 10 mM Tris-HCl, pH 8.0 with 10 mM pyridoxal 5'-phosphate, with 0.1 M bis-tris pH 7.0, 22% w/v PEG 4000, X-ray diffraction structure determination and analysis at 2.6 A resolution
purified recombinant His-tagged wild-type enzyme in complex with L-alanine and pyridoxal 5'-phosphate, hanging drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 10 mM Tris-HCl, pH 8.0, L-Ala and PLP at 1:1.5:1.5 molar ratio, with 0.001 ml of reservoir solution containing 22% PEG 4000, and 0.1 M Bis-Tris, pH 7.0, and equilibration against 0.3 ml reservoir solution, 16°C, X-ray diffraction structure determination and analysis at 2.7 A resolution, molecular replacement using the alanine racemase from Bacillus stearothermophilus, PDB ID 1SFT, as a search model
wild-type enzyme in complex with pyridoxal-5'-phosphate or with D-cycloserine, and enzyme mutant K271T in complex with pyridoxal 5'-phosphate, sitting drop vapor diffusion method, mixing of 0.002 ml of 32 m/ml protein in 10 mM PLP, 1 mM TCEP, and 50 mM Tris-HCl, pH 8.0, with 0.0015 ml of reservoir solution containing 0.2 M ammonium sulfate, 0.1 M Bis-Tris, pH 6.5, 25% w/v PEG 3350 for the wild-type/PLP complex, and additional 100 mM cycloserine, 200 mM sodium formate, 20% w/v PEG 3350 for the wild-type enzyme/inhibitor complex, or containing 0.17 M lithium sulfate, 0.085 M Tris-HCl, pH 8.5, 25.5% w/v PEG 4000, and 20% v/v glycerol for the enzyme mutant/PLP complex, X-ray diffraction structure determination and analysis at 2.1-2.6 A resolution
hanging-drop vapor-diffusion method, protein concentration: 20 mg/ml; crystal screen buffer: 0.1 M HEPES, pH 8.0, 22% (w/v) PEG 8000, 0.3 M Ca-acetate, and 1/10 (v/v) cyclohexyl-methyl-beta-D-maltoside, drop: ratio 1/2 mixed protein solution and buffer (sum 2 microl) hanging over 1 ml of buffer; cryo-protecting solution: 0.1 M HEPES, pH 8.0, 22% (w/v) PEG 8000, 0.3 M Ca-acetate, 30% (v/v) glycerol and 1/10 (v/v) cyclohexyl-methyl-beta-D-maltoside for flashcooling in liquid nitrogen, diffracted to 2.5 A
-
enzyme in complex with pyridoxyl 5'-phosphate and inhibitor acetate, PDB ID 1SFT
-
hanging drop method using purified enzyme concentrated to 22 mg/ml. The hanging drop contains 0.01 ml of the protein solution, 0.01 ml of 23% polyethylene glycol 4K, 200 mM sodium acetate and 100 mM Tris, pH 8.5. Drops are equilibrated against 0.7 ml of polyethylene glycol 4K solution
hanging drop method, determination of the crystal structure of the (R)-1-aminoethylphosphonic acid-pyridoxal 5'-phosphate aldimine in complex with alanine racemase at 1.6 A resolution
hanging drop method, the structure of the enzyme with the inhibitor propionate bound in the active site is determined by X-ray crystallography to a resolution of 1.9 A
hanging-drop vapor diffusion method. Crystal structure of the enzyme bound with reaction intermediate analogs, N-(5'-phosphopyridoxyl)-L-alanine and N-(5'-phosphopyridoxyl)-D-alanine, determined at 2.0 A resolution with the crystallographic R factor of 17.2 for PLP-L-Ala and 16.9 for PLP-D-Ala complexes
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mutant Y265F in complex with D- and with L-cycloserine
study of water molecules by cluster analysis of several crystal structures
purified recombinant C-terminally His6-tagged selenomethionine-derivatized enzyme by sitting drop vapour diffusion method, mixing of 0.002 ml of 10 mg/ml protein solution with 0.002 ml of reservoir solution containing 25% PEG 3350, 0.1 M Bis-Tris, pH 5.5, 0.2 M sodium chloride, and equilibration against 0.650 ml of reservoir solution, X-ray diffraction structure determination and analysis at 1.7 A resolution via single wavelength anomalous dispersion
sitting drops equilibrated versus 1.5 M (NH4)2SO4, 2% polyethylene glycol 400 and 0.1 M HEPES, pH 7.5, crystal strcuture at 1.45 A resolution
purified recombinant enzyme from strain Mu50, sitting drop method, mixing of 12 mg/ml protein in 20 mM Tris-HCl, pH 7.6, with 100 mM sodium acetate trihydrate, pH 5.0, and 1.8 M ammonium sulfate, 7 days, X-ray diffraction structure determination and analysis at 2.15 A resolution, molecular replacement
sitting drop vapor diffusion method
sitting drop vapor diffusion method, at 4°C in 1.2 M sodium citrate, 0.1 M MES, pH 7.2, and 10% (v/v) glycerol
purified recombinant N-terminally His-tagged enzyme free, or in complex with inhibitors D-cycloserine and propionate, sitting drop vapor diffusion, mixing of 0.001 ml of 20 mg/ml protein solution with 0.001 ml of crystallization solution containing 0.1 M Bis-Tris propane, pH 8.5, 0.2 M NaBr, 20% w/v PEG 3350, 38 days, X-ray diffraction structure determination and analysis at 2.8 A for the free enzyme, and at 1.51-1.64 A resolution for the enzyme complexes, model building
free enzyme and in complex with D- or L-cycloserine
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