牛谷氨酸脱氢酶的催化活性需要六聚体结构。
Catalytic activity of bovine glutamate dehydrogenase requires a hexamer structure.
作者信息
Bell E T, Bell J E
出版信息
Biochem J. 1984 Jan 1;217(1):327-30. doi: 10.1042/bj2170327.
Abstract
Previous workers have shown that the hexamers of glutamate dehydrogenase are dissociated first into trimers and subsequently into monomers by increasing guanidinium chloride concentrations. In renaturation experiments it is shown that trimers of glutamate dehydrogenase can be reassociated to give the hexamer form of the enzyme, with full regain of activity. Monomeric subunits produced at high guanidinium chloride concentrations cannot be renatured. The trimer form of the enzyme is shown to have no catalytic activity, although the hexamer form in guanidinium chloride has full activity.
摘要
先前的研究人员已经表明，谷氨酸脱氢酶的六聚体首先会通过增加氯化胍的浓度解离成三聚体，随后再解离成单体。在复性实验中发现，谷氨酸脱氢酶的三聚体可以重新结合形成该酶的六聚体形式，并完全恢复活性。在高浓度氯化胍条件下产生的单体亚基无法复性。尽管氯化胍中的六聚体形式具有完全活性，但该酶的三聚体形式却没有催化活性。
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