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5.1.1.13: aspartate racemase

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

Word Map on EC 5.1.1.13

Reaction

L-aspartate
=
D-Aspartate

Synonyms

Asp racemase, Aspartate racemase, AspR, D-Asp racemase, D-Aspartate racemase, GOT1L1, LsAspR, OCC_11152, P. AspR, PhAspR, PLP-independent AspR, PTO0149, PtoAspR, pyridoxal 5'-phosphate independent aspartate racemase, pyridoxal 5'-phosphate-independent aspartate racemase, Racemase, aspartate, SbAspR, Tl-AspR

ECTree

     5 Isomerases
         5.1 Racemases and epimerases
             5.1.1 Acting on amino acids and derivatives
                5.1.1.13 aspartate racemase

Crystallization

Crystallization on EC 5.1.1.13 - aspartate racemase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme, hanging drop vapour diffusion method, mixing of 0.006 ml of 2.5 mg/ml protein in 10 mM Tris-HCl, 20 mM pyridoxal 5'-phosphate, 1 mM 2-mercaptoethanol, pH 8.8, with 0.003 ml of reservoir solution containing 27% w/v PEG 4000, 50 mM sodium acetate, pH 5.0, 200 mM ammonium acetate, and 15% v/v glycerol, and equilibration against 0.1 ml of reservoir solution, 14°C, X-ray diffraction structure determination and analysis at 1.90 A resolution
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purified enzyme, sitting drop vapour diffusion method with microseeding, mixing of 0.002 ml of 20 mg/ml protein in 50 mM MES, pH 6.5, and 4 mM dithiothreitol, with 0.002 ml of reservoir solution containing 25% v/v PEG MME 550, and 5% v/v 2-propanol, and 0.1 M sodium acetate, pH 4.8, equilibration againat 0.1 ml reservoir solution, 20°C, single rod-shaped crystals, X-ray diffraction structure determination and analysis at 2.55 A resolution, molecular replacement calculations are carried out using the coordinates of PhAspR, PDB ID 1jfl, as a starting model
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purified recombinant enzyme, vapour diffusion method, mixing of 8-12 mg/ml protein in 50 mM Tris-HCl, pH 8.0, with reservoir solution containing 20-25% w/v PEG 3400, 200 mM potassium/sodium tartrate, and 1 mM L-aspartate, X-ray diffraction structure determination and analysis at 1.85 A resolution, molecular replacement method using the structure of aspartate racemase from Salmonella typhimurium, PDB ID 3S81, as a probe model
catalytically inactive mutant C82A in complex with citric acid, 2.0 A resolution. Citric acid binds to the catalytic site, which induces a conformational change to close the active site. Residue R48 is responsible for recognizing carboxyl groups of the substrates L-/D-aspartates and stabilizing a reaction intermediate, and L164 is responsible for stabilizing a closed state structure
sitting drop vapour diffusion method at 293 K, space group P21 with a: 65.5 A, b: 58.7 A, c: 67 A and beta 109.6°
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sitting drop vapour diffusion method at 293 K, space groups: P21 with a: 65.5 A, b: 58.7 A, c: 67.0 A, and beta: 109.6°, P212121 with a: 68.1 A, b: 135 A and c: 151.5 A, and P3121 with a and b: 80.6 A and c: 70.3 A
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