EC Number   |
Reference |
|---|
   1.1.1.B20 | in complex with substrate meso-2,3-butanediol and inhibitor 2-mercaptoethanol, to 1.7 A resolution. The overall structure is similar to that of other short chain dehydrogenase/reductase enzymes, the NAD+ binding site, and the positions of catalytic residues Ser139, Tyr152, and Lys156 are also conserved. 2-Mercaptoethanol forms hydrogens bonds with residues Gln 140 and Gly 183 close to the active site, which are important but not sufficient for distiguishing stereoisomerism of a chiral substrate |
246405 |
| 1.1.1.B20 | recombinant wild-type and mutant SmBdh proteins in complex with NAD+ and acetoin both bound in the active site, sitting drop vapor diffusion method, protein solution for wild-type SmBdh contains 9 mg/ml of protein, 20 mM Tris, pH 7.5, 100 mM NaCl, 20 mM NAD+, and 200 mM acetoin, the protein solution for mutant SmBdh Q247A consists of 4.2 mg/ml of protein, 20 mM Tris, pH 7.5, 100 mM NaCl, 20 mM NAD+, and 20 mM acetoin, and for mutant SmBdh Q247V/V139Q of 14.5 mg/ml of protein, 20 mM Tris, pH 7.5, 100 mM NaCl, 20 mM NAD+, and 20 mM acetoin, the well solution contains 0.1 M sodium malonate, pH 6-7 and 6-15% w/v PEG 3350, mixing of 200 nl of protein with 100-300 nl of well solution, equilibration against 0.05 ml of well solution, 20°C, X-ray diffraction structure determination and analysis at 1.8-2.0 A resolution |
760761 |
| 1.1.1.B20 | recombinant wild-type and mutant SmBdh proteins in complex with with NAD+ and acetoin both bound in the active site, sitting drop vapor diffusion method, protein solution for wild-type SmBdh contains 9 mg/ml of protein, 20 mM Tris, pH 7.5, 100 mM NaCl, 20 mM NAD+, and 200 mM acetoin, the protein solution for mutant SmBdh Q247A consists of 4.2 mg/ml of protein, 20 mM Tris, pH 7.5, 100 mM NaCl, 20 mM NAD+, and 20 mM acetoin, and for mutant SmBdh Q247V/V139Q of 14.5 mg/ml of protein, 20 mM Tris, pH 7.5, 100 mM NaCl, 20 mM NAD+, and 20 mM acetoin, the well solution contains 0.1 M sodium malonate, pH 6-7 and 6-15% w/v PEG 3350, mixing of 200 nl of protein with 100-300 nl of well solution, equilibration against 0.05 ml of well solution, 20°C, X-ray diffraction structure determination and analysis at 1.8-2.0 A resolution |
760761 |
