EC Number |
Reference |
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1.3.8.7 | 5-10 mg/ml enzyme in 50 mM potassium phosphate, pH 7.5, 0.1 mM EDTA, 2% polyethylene glycol 6000, 4°C, after 7 days 5% polyethylene glycol, crystals emerge 2-3 days later |
391356 |
1.3.8.7 | dialysis against distilled water at 4°C |
391351 |
1.3.8.7 | FT-IR spectroscopic studies. The hydrogen-bond enthalpy change responsible for the polarization on the transfer of the substrate from aqueous solution to the active site of enzyme is estimated to be 15 kcal/mol. The 1626 per cm band is noticeably weakened in the case of acyl-CoA with acyl chains longer than C12 which are poor substrates, suggesting that C(1) =O is likely to exist in multiple orientations in the active-site cavity, whence the band becomes obscured. A band identical to that of bound C8-CoA is observed in the case of C4-CoA which is a poor substrate, indicating the strong hydrogen bond at C(1)-O |
698667 |
1.3.8.7 | molecular dynamics simulation and comparison between the porcine MCAD and human MCAD structures. Both proteins are essentially similar |
742255 |
1.3.8.7 | sitting-drop method, native enzyme and enzyme-substrate complex, x-ray structure, 2.4 A resolution, monomer is folded into 3 domains of approx. equal size, the flavin ring is located in a crevice between the beta-domain and the C-terminal domain |
391365 |
1.3.8.7 | wild-type and E376G/T255E double mutant enzyme and enzyme substrate complexes, vapor diffusion method at 4°C using the sitting drop technique, 0.027 mg enzyme in 140 mM Tris-acetate, pH 7.0, 8% w/v polyethylene glycol 4000, the human enzyme structure is essentially the same as that of the pig enzyme |
391368 |
1.3.8.7 | x-ray structure, 3.0 A resolution |
391318 |