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Results 1 - 7 of 7
EC Number Crystallization (Commentary) Reference
Show all pathways known for 1.3.8.7Display the word mapDisplay the reaction diagram Show all sequences 1.3.8.75-10 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
Show all pathways known for 1.3.8.7Display the word mapDisplay the reaction diagram Show all sequences 1.3.8.7dialysis against distilled water at 4°C 391351
Show all pathways known for 1.3.8.7Display the word mapDisplay the reaction diagram Show all sequences 1.3.8.7FT-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
Show all pathways known for 1.3.8.7Display the word mapDisplay the reaction diagram Show all sequences 1.3.8.7molecular dynamics simulation and comparison between the porcine MCAD and human MCAD structures. Both proteins are essentially similar 742255
Show all pathways known for 1.3.8.7Display the word mapDisplay the reaction diagram Show all sequences 1.3.8.7sitting-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
Show all pathways known for 1.3.8.7Display the word mapDisplay the reaction diagram Show all sequences 1.3.8.7wild-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
Show all pathways known for 1.3.8.7Display the word mapDisplay the reaction diagram Show all sequences 1.3.8.7x-ray structure, 3.0 A resolution 391318
Results 1 - 7 of 7