Pons M, Michel F, Descomps B, Crastes de Paulet A
Eur J Biochem. 1978 Mar;84(1):257-66. doi: 10.1111/j.1432-1033.1978.tb12164.x.
The inhibition of glutamate dehydrogenase by estrogens, estrogen analogues or polyphenylethylene derivatives (about one hundred molecules, most of them having estrogenic or antiestrogenic activities) was measured. The efficiency of these compounds in inducing allosteric inhibition of the enzyme was compared and correlated to their chemical structure: an aromatic ring A, a free phenolic group in the region of carbon 3 of the steroid nucleus and a lipophilic substitution in the region of C-12, C-13 or C-17 were found to be the main structural features required for maximal efficiency on glutamate dehydrogenase. A tentative model for the relative orientation of the main inhibitor families is proposed. It accounts for most of the kinetic results and can be used as a tool for the selection of affinity labels directed towards the estrogen binding site of glutamate dehydrogenase.
测定了雌激素、雌激素类似物或聚苯乙烯衍生物（约一百种分子，其中大多数具有雌激素或抗雌激素活性）对谷氨酸脱氢酶的抑制作用。比较了这些化合物诱导该酶变构抑制的效率，并将其与化学结构相关联：发现一个芳香A环、甾体核碳3区域的一个游离酚羟基以及C-12、C-13或C-17区域的亲脂性取代基是对谷氨酸脱氢酶产生最大抑制效率所需的主要结构特征。提出了主要抑制剂家族相对取向的初步模型。该模型解释了大部分动力学结果，可作为选择针对谷氨酸脱氢酶雌激素结合位点的亲和标记物的工具。
