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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selection
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Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selection

机译：具有盖门控活性位点的酶必须通过诱导拟合机制运行，而不是构象选择

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摘要

The induced fit and conformational selection/population shift models are two extreme cases of a continuum aimed at understanding the mechanism by which the final key-lock or active enzyme conformation is achieved upon formation of the correctly ligated enzyme. Structures of complexes representing the Michae-lis and enolate intermediate complexes of the reaction catalyzed by phosphoenolpyruvate carboxykinase provide direct structural evidence for the encounter complex that is intrinsic to the induced fit model and not required by the conformational selection model. In addition, the structural data demonstrate that the conformational selection model is not sufficient to explain the correlation between dynamics and catalysis in phosphoenolpyruvate carboxykinase and other enzymes in which the transition between the uninduced and the induced conformations occludes the active site from the solvent. The structural data are consistent with a model in that the energy input from substrate association results in changes in the free energy landscape for the protein, allowing for structural transitions along an induced fit pathway.
机译：诱导的适应和构象选择/种群转移模型是连续体的两个极端情况，旨在了解形成正确连接的酶后最终键锁或活性酶构象的机理。表示烯醇丙酮酸丙酮酸羧激酶催化反应的Michae-lis和烯醇中间体复合物的复合物结构为所遇到的复合物提供了直接的结构证据，这是诱导的拟合模型所固有的，而构象选择模型并不需要。另外，结构数据表明，构象选择模型不足以解释磷酸烯醇丙酮酸羧化激酶和其他酶的动力学与催化之间的相关性，其中未诱导构象和诱导构象之间的转变将活性位点从溶剂中封闭。结构数据与模型一致，因为来自底物缔合的能量输入会导致蛋白质的自由能格局发生变化，从而允许沿着诱导的拟合路径进行结构转变。

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