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本文培养了三种Palinurus versicolor龙虾肌肉D-甘油醛-3-磷酸脱氢酶的晶体:脱辅基酶、脱辅基羧甲基酶和每四体含两个荧光NAD衍生物的酶晶体。用X射线衍射法测定了它们的空间群与晶胞参数。结果表明这些晶体以及对应的为NAD~+所饱和的holo酶晶体彼此同晶,良好的同晶性提示着,此种种属来源的甘油醛-3-磷酸脱氢酶与辅酶的结合不大可能导致如同Bacillus stearothermophillus酶那样涉及结构域相对运动的较大幅度的构象变化。
In this paper, three crystals of D-glyceraldehyde-3-phosphate dehydrogenase from Loblind muscle of Palinurus versicolor were cultured: apoenzyme, apo-carboxymethyl enzyme and enzyme crystal containing two fluorescent NAD derivatives per four body. Their space group and unit cell parameters were determined by X-ray diffraction. The results show that these crystals and corresponding holo enzyme crystals saturated with NAD ~ + are isomorphic to each other, and good isomorphism suggests that the combination of glyceraldehyde-3-phosphate dehydrogenase from this species with coenzyme is less likely Resulting in a more substantial conformational change involving the relative movement of the domains as the Bacillus stearothermophillus enzyme does.