酶催化过程中的构象变化：水在过渡态中的作用。
Conformational changes during enzyme catalysis: role of water in the transition state.
作者信息
Loftfield R B, Eigner E A, Pastuszyn A, Lövgren T N, Jakubowski H
出版信息
Proc Natl Acad Sci U S A. 1980 Jun;77(6):3374-8. doi: 10.1073/pnas.77.6.3374.
Abstract
The entropy of activation for the synthesis of Ile-tRNA is high and positive. The only likely source of a high delta S is the loss of structured water as the enzyme . substrate complex moves toward the transition state. This requires a change in the orientation or nature of water-organizing residues in the interface between the enzyme . substrate complex and the water. Such changes, which may be some distance from the "active site," are coupled to the active site in such a way that the increased entropy and decreased free energy of the water--enzyme interface is available at the "active site" to reduce the free energy of activation. The effects of Hofmeister anions on KmS and KcatS are consistent with the entropy data.
摘要
异亮氨酰 - tRNA合成的活化熵很高且为正值。高ΔS的唯一可能来源是当酶 - 底物复合物向过渡态转变时结构化水的丢失。这需要酶 - 底物复合物与水之间界面处水组织残基的取向或性质发生变化。这种变化可能距离“活性位点”有一段距离，它与活性位点以这样一种方式耦合，即水 - 酶界面增加的熵和降低的自由能在“活性位点”处可用，以降低活化自由能。霍夫迈斯特阴离子对KmS和KcatS的影响与熵数据一致。
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