Lascu I, Bârzu T, Ty N G, Ngoc L D, Bârzu O, Mantsch H H
Biochim Biophys Acta. 1977 Jun 10;482(2):251-60. doi: 10.1016/0005-2744(77)90239-x.
A total of 26 different purine nucleotides with specific modifications in the base moiety and/or in the polyphosphate chain as well as various combinations of nucleotides were tested as allosteric effectors of beef liver glutamate dehydrogenase (L-glutamate : NAD(P)+ oxidoreductase (deaminating), EC 1.4.1.3). The capacity of these nucleotide analogs to activate or to inhibit the glutamate dehydrogenase activity is expressed quantitatively and scaled between the extreme effects of ADP and GTP, respectively. The significance of distinct structural elements for the enzyme-effector interaction is discussed. While the inhibitory GTP site is less specific, accepting many natural and most modified nucleoside triphosphates as inhibitors, the activating ADP site shows a much higher specificity for nucleotides as activators.
总共测试了26种在碱基部分和/或多磷酸链上有特定修饰的不同嘌呤核苷酸以及各种核苷酸组合，作为牛肝谷氨酸脱氢酶（L-谷氨酸：NAD(P)+氧化还原酶（脱氨基），EC 1.4.1.3）的变构效应剂。这些核苷酸类似物激活或抑制谷氨酸脱氢酶活性的能力以定量方式表示，并分别在ADP和GTP的极端效应之间进行缩放。讨论了不同结构元件对酶-效应剂相互作用的重要性。抑制性GTP位点的特异性较低，接受许多天然和大多数修饰的核苷三磷酸作为抑制剂，而激活性ADP位点对作为激活剂的核苷酸表现出更高的特异性。
