Ding Wei, Li Yongzhen, Zhang Qi
Department of Chemistry, Fudan University, Shanghai 200433, China.
ACS Chem Biol. 2015 Jul 17;10(7):1590-8. doi: 10.1021/acschembio.5b00104. Epub 2015 Apr 20.
Enzymes are generally believed to be highly regio- and stereoselective catalysts that strictly control the reaction coordinates and dominate the final catalytic outcomes. However, recent studies have started to suggest that substrates sometimes play key roles in determining the product selectivity in enzyme catalysis. Here, we highlight several enzymatic reactions in which the stereoselectivity is, at least in large part, governed by the intrinsic properties of the substrate rather than by characteristics of the enzyme. These reactions are involved in the biosynthesis of different classes of natural products, including lanthipeptides, sactipeptides, and polyketides. Understanding the mechanism of substrate-controlled stereospecificity may not only expand our knowledge of enzyme catalysis and enzyme evolution but also guide bioengineering efforts to produce novel valuable products.
酶通常被认为是高度区域和立体选择性的催化剂，能严格控制反应坐标并主导最终的催化结果。然而，最近的研究开始表明，底物有时在酶催化中决定产物选择性方面起着关键作用。在这里，我们重点介绍了几个酶促反应，其中立体选择性至少在很大程度上是由底物的内在性质而非酶的特性所决定的。这些反应参与了不同类别的天然产物的生物合成，包括羊毛硫肽、硫肽和聚酮化合物。了解底物控制的立体特异性机制不仅可以扩展我们对酶催化和酶进化的认识，还可以指导生物工程努力生产新型有价值的产品。
