构象变化与谷氨酸脱氢酶活性的调节
Conformational changes and the regulation of glutamate-dehydrogenase activity.
作者信息
Bayley P M, Radda G K
出版信息
Biochem J. 1966 Jan;98(1):105-11. doi: 10.1042/bj0980105.
Abstract
- The effect of NADH and the non-competitive inhibitor GTP on the optical-rotatory-dispersion properties of glutamate dehydrogenase has been studied. 2. Analysis of the data in terms of the a(0) and b(0) parameters of the Moffitt-Yang equation indicates that a conformational change is induced either by NADH or by GTP in the presence of small amounts of NADH. 3. Sedimentation measurements under comparable conditions showed that the enzyme reversibly dissociates into sub-units but that this dissociation is only secondary to the conformational changes. 4. Fluorescence measurements showed that the binding constant of NADH and the number of binding sites on the enzyme increased in the presence of GTP. 5. This is confirmed by studies of fluorescence polarization, which in addition showed that the movement of NADH on the enzyme surface is more restricted in the presence of GTP. 6. The relation of these results to possible regulatory mechanisms is discussed.
摘要
- 研究了NADH和非竞争性抑制剂GTP对谷氨酸脱氢酶旋光色散特性的影响。2. 根据莫菲特-杨方程的a(0)和b(0)参数对数据进行分析，结果表明，在少量NADH存在的情况下，NADH或GTP均可诱导构象变化。3. 在可比条件下进行的沉降测量表明，该酶可逆地解离为亚基，但这种解离仅是构象变化的次要结果。4. 荧光测量表明，在GTP存在时，NADH的结合常数和酶上的结合位点数增加。5. 荧光偏振研究证实了这一点，此外还表明，在GTP存在时，NADH在酶表面的移动受到更多限制。6. 讨论了这些结果与可能的调节机制的关系。
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