School of Chemistry, National University of Ireland, Galway, Galway, Ireland.
Biochemistry. 2013 Aug 20;52(33):5511-3. doi: 10.1021/bi400546j. Epub 2013 Aug 9.
The stereospecificity of d-glucarate dehydratase (GlucD) is explored by QM/MM calculations. Both the substrate binding and the chemical steps of GlucD contribute to substrate specificity. Although the identification of transition states remains computationally intensive, we suggest that QM/MM computations on ground states or intermediates can capture aspects of specificity that cannot be obtained using docking or molecular mechanics methods.
通过量子力学/分子力学(QM/MM)计算探索了 D-葡萄糖醛酸脱水酶(GlucD)的立体专一性。底物结合和 GlucD 的化学步骤都有助于底物特异性。尽管过渡态的确定仍然计算密集，但我们认为，对基态或中间体的 QM/MM 计算可以捕捉到使用对接或分子力学方法无法获得的特异性方面。
