Yon J M, Perahia D, Ghélis C
Laboratoire de Modélisation et d'Ingénérie des Protéines, Unité Associée du CNRS, Université de Paris-Sud, Orsay, France.
Biochimie. 1998 Jan;80(1):33-42. doi: 10.1016/s0300-9084(98)80054-0.
Conformational flexibility and structural fluctuations play an important role in enzyme activity. A great variety of internal motions ranging over different time scales and of different amplitudes are involved in the catalytic cycle. These different types of motions and their functional consequences are considered in the light of experimental data and theoretical analyses. The conformational changes upon substrate binding, and particularly the hinge-bending motion which occurs in enzymes made of two domains, are analyzed from several well documented examples. The conformational events accompanying the different steps of the catalytic cycle are discussed. The last section concerns the motions involved in the allosteric transition which regulates the enzyme activity.
构象灵活性和结构波动在酶活性中起着重要作用。催化循环涉及各种不同时间尺度和不同幅度的内部运动。根据实验数据和理论分析，考虑了这些不同类型的运动及其功能后果。从几个有充分文献记载的例子中分析了底物结合时的构象变化，特别是在由两个结构域组成的酶中发生的铰链弯曲运动。讨论了催化循环不同步骤伴随的构象事件。最后一部分涉及调节酶活性的变构转变中涉及的运动。
