Popova S V, Sugrobova N P
Biokhimiia. 1983 Nov;48(11):1783-7.
The effects of coenzymes NAD(P) and NAD(P)H on the kinetics of the ox liver glutamate dehydrogenase reaction have been studied. The oxidized coenzymes were shown to activate alpha-ketoglutarate amination at inhibiting concentrations of NADH and NADPH. The reduced coenzymes, NADH and NADPH, inhibit glutamate deamination with both NAD and NADP as coenzymes. The data obtained are discussed in terms of literature data on the mechanisms of the coenzyme effects on the glutamate dehydrogenase activity and are inconsistent with the theory of direct ligand--ligand interactions. It was shown that the peculiarities of the glutamate dehydrogenase kinetics can easily be interpreted in the light of the two state models.
已对辅酶NAD(P)和NAD(P)H对牛肝谷氨酸脱氢酶反应动力学的影响进行了研究。结果表明，在NADH和NADPH的抑制浓度下，氧化型辅酶可激活α-酮戊二酸胺化反应。还原型辅酶NADH和NADPH在以NAD和NADP为辅酶时抑制谷氨酸脱氨反应。根据关于辅酶对谷氨酸脱氢酶活性影响机制的文献数据对所得数据进行了讨论，这些数据与直接配体-配体相互作用理论不一致。结果表明，根据双态模型可以很容易地解释谷氨酸脱氢酶动力学的特性。
