EC Number |
---|
2.3.1.41 | - |
2.3.1.41 | comparison of crystal structures of the active sites of Escherichia coli KAS I with human cytosolic acetoacetyl-CoA thiolase and bacterial thiolase, overview |
2.3.1.41 | enzyme in complex with platencin, 7-hydroxycoumarin, and (5-thiophen-2-ylisoxazol-3-yl)methanol, using 20% (w/v) PEG 3350, 100 mM bis-Tris propane pH 8.5, 200 mM sodium malonate |
2.3.1.41 | hanging drop vapour diffusion method, protein solution: 25 mM Tris-HCl, pH 8.0, 300 mM NaCl, 75 mM imidazole, reservoir solution: 0.085 M tri-sodium citrate, 0.17 M ammonium acetate, 22% w/v polyethylene glycol 4000, 15% v/v glycerol as cryo-protectant, 15% w/v 1,2,3-heptanetriol, x-ray structure analysis, three-dimensional model |
2.3.1.41 | hanging-drop vapour-diffusion method, ammonium sulfate |
2.3.1.41 | in complex with Escherichia coli acyl-carrier protein, sitting drop vapor diffusion method, using 0.1 M sodium acetate pH 5.4, 0.2 M ammonium acetate, and 20% (w/v) PEG 4000 |
2.3.1.41 | in complex with lauroyl-CoA |
2.3.1.41 | purified recombinant enzyme free or complexed with acyl-CoA, hanging drop vapour diffusion method, 0.002 ml of protein solution, containing 0.087 mg of protein with or without 4 mM hexanoyl-CoA, mixed with 0.002 ml of reservoir solution containing 24% w/v PEG 3350 and 0.2 M NH4Cl, 5-8 days at room temperature, rod-shaped single crystals, X-ray diffraction structure determination and analysis at 1.6 A resolution, structure modeling |
2.3.1.41 | purified recombinant wild-type and mutant enzymes, free or bound to C8 and C12, respectively, X-ray diffraction structure determination and analysis at 1.8-2.4 A resolution |
2.3.1.41 | structure analysis, three-dimensional model of enzyme complexed with inhibitors thiolactomycin and cerulenin |