EC Number   |
|---|
    2.2.1.6 | - |
| 2.2.1.6 | crystal structure analysis |
| 2.2.1.6 | free enzyme and in complex with inhibitors, hanging drop vapor diffusion method, using 1 M sodium potassium tartrate, 0.1 M CHES and 0.1-0.2 M lithium sulfate |
| 2.2.1.6 | homology modeling of enzyme based on the structure of the yeast enzyme.In the model, the S167 and S506 residues lie near the FAD binding site, while the S539 residue is found near the thiamine diphosphate binding site |
| 2.2.1.6 | in complex with inhibitors N-[(4-methylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide and methyl 2-([(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl)benzoate, to 3.0 A and 2.8 A resolution, respectively. In both complexes, the inhibitors are bound in the tunnel leading to the active site, such that the sole substituent of the heterocyclic ring is buried deepest and oriented towards the thiamine diphosphate. The cofactor is intact and present most likely as the hydroxylethyl intermediate |
| 2.2.1.6 | in complex with penoxsulam, hanging drop vapor diffusion method, using 1.0 M succinic acid, pH 7.0, 0.1 M HEPES, pH 7.0, and 1% (w/v) PEG monomethyl ether 2000 |
| 2.2.1.6 | in complex with propoxycarbazone or thiencarbazone methyl, hanging drop vapor diffusion method, using 1.0 M Na/K tartrate, 0.1 M CHES, and 0.19 M (NH4)2SO4. In complex with bispyribac or pyrithiobac, hanging drop vapor diffusion method, using 20% (w/v) PEG 3350 and 0.2 M sodium citrate tribasic dihydrate or 0.2 M potassium citrate tribasic dihydrate |
| 2.2.1.6 | in complex with pyruvate |
| 2.2.1.6 | purified enzyme in the presence of thiamine diphosphate and Mg2+, and in a transition state with a 2-lactyl moiety bound to thiamine diphosphate, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement |
| 2.2.1.6 | purified recombinant wild-type and selenomethionine-labeled isozyme AHAS III in complex with valine, hanging drop vapour diffusion method, room temperature, 0.0036 ml of protein solution containing 10-25 mg/ml protein and 0.5 M MgCl2, is mixed with reservoir solution containing 30-40% PEG 400, 0.4-0.6 M MgCl2, 100 mM Tris-HCl, pH 8.5, tetragonal or orthorhombic crystals, X-ray diffraction structure determination and analysis at 1.75-2.5 A resolution |
