Warwicker J
Food Macromolecular Science Department, Institute of Food Research, Reading Laboratory, UK.
FEBS Lett. 1997 Mar 10;404(2-3):159-63. doi: 10.1016/s0014-5793(97)00119-1.
Electrostatic calculations predict that amino-terminal conformation and ionisation contribute significantly to transition state stability in phospholipase A2, so that control of these factors by binding to aggregated substrate provides a plausible mechanism for interfacial activation. In particular, it is suggested that a part of the pH dependence of interfacial activity may arise from transient deprotonation of an ordered amino-terminus. Interface charge and the detailed structure of the interfacial complex are also predicted to influence catalytic activity. The model is compared with available biochemical data.
静电计算预测，氨基末端的构象和电离对磷脂酶A2过渡态稳定性有显著贡献，因此通过与聚集底物结合来控制这些因素为界面激活提供了一种合理的机制。特别指出，界面活性对pH的依赖性部分可能源于有序氨基末端的瞬时去质子化。界面电荷和界面复合物的详细结构预计也会影响催化活性。该模型与现有的生化数据进行了比较。
