Organic Chemistry Department, University of Salamanca, Plaza de los Caídos s/n, 37008, Salamanca, Spain.
X-Ray Diffraction Analysis Department, University of Salamanca, Plaza de los Caídos s/n, 37008, Salamanca, Spain.
Angew Chem Int Ed Engl. 2022 Aug 26;61(35):e202206072. doi: 10.1002/anie.202206072. Epub 2022 Jun 7.
The synthesis of small molecules able to mimic the active site of hydrolytic enzymes has been largely pursued in recent decades. The high reaction rates and specificity shown by natural hydrolases present an attractive target, and yet the preparation of suitable small-molecule mimics remains challenging, requiring activated substrates to achieve productive outcomes. Here we present small synthetic artificial enzymes which mimic the catalytic site and the oxyanion hole of chymotrypsin and N-terminal hydrolases and are able to perform, for the first time, the transesterification of a non-activated ester such as ethyl acetate with methanol under mild and neutral reaction conditions.
在过去几十年中，人们大力研究能够模拟水解酶活性部位的小分子的合成。天然水解酶所表现出的高反应速率和特异性是一个很有吸引力的目标，但制备合适的小分子模拟物仍然具有挑战性，需要激活底物才能产生有效的结果。在这里，我们提出了一些小型的人工合成酶，它们模拟了糜蛋白酶和 N 端水解酶的催化部位和氧阴离子空穴，并且首次能够在温和中性的反应条件下，使非激活酯（如乙酸乙酯）与甲醇进行酯交换反应。
