谷氨酸脱氢酶的动力学研究。2-氧代戊二酸的还原胺化作用。
Kinetic studies of glutamate dehydrogenase. The reductive amination of 2-oxoglutarate.
作者信息
Engel P C, Dalziel K
出版信息
Biochem J. 1970 Jul;118(3):409-19. doi: 10.1042/bj1180409.
Abstract
- Kinetic studies of the reductive amination of 2-oxoglutarate catalysed by glutamate dehydrogenase with NADH and NADPH as coenzyme were made at pH7.0 and pH 8.0. The concentrations of both substrates and coenzymes were simultaneously varied over wide ranges. Lineweaver-Burk plots with respect to each substrate and coenzyme were linear, except that with high concentrations of 2-oxoglutarate or coenzyme inhibition occurred. There was no evidence of the negative homotropic interactions between the enzyme subunits that were revealed in previous kinetic studies of the reverse reaction. 2. The initial-rate results are shown to be inconsistent with any of the six possible compulsory-order mechanisms for this three-substrate reaction, and it is concluded that a random-order mechanism is the most likely one. On the basis of this mechanism, the dissociation constants of all the binary, ternary and quaternary complexes of the enzyme and substrates are calculated from initial-rate parameters. 3. The results are discussed in relation to those of earlier workers who concluded that the mechanism is of the compulsory-order type.
摘要
- 以NADH和NADPH作为辅酶，在pH7.0和pH8.0条件下对谷氨酸脱氢酶催化的2-氧代戊二酸还原胺化反应进行了动力学研究。两种底物和辅酶的浓度在很宽的范围内同时变化。除了在高浓度的2-氧代戊二酸或辅酶存在时出现抑制作用外，针对每种底物和辅酶的林-贝氏图均呈线性。在先前该反应逆向反应的动力学研究中所揭示的酶亚基之间的负同促相互作用没有证据。2. 初始速率结果表明与该三底物反应的六种可能的强制顺序机制中的任何一种均不一致，并且得出结论，随机顺序机制是最有可能的。基于该机制，根据初始速率参数计算酶与底物的所有二元、三元和四元复合物的解离常数。3. 结合早期研究者得出该机制为强制顺序类型的结果对这些结果进行了讨论。
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