Dynamic Tuning in Synthetic Glycosidase for Selective Hydrolysis of Alkyl and Aryl Glycosides.
Dynamic Tuning in Synthetic Glycosidase for Selective Hydrolysis of Alkyl and Aryl Glycosides.
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动态调节合成糖苷酶选择性水解烷基和芳基糖苷。
DOI：
10.1021/acs.joc.1c03029
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发表时间：
2022-03-18
影响因子：
3.6
通讯作者：
Zhao, Yan
中科院分区：
文献类型：
--
作者：
Chen, Kaiqian;Zhao, Yan
酶使用复杂的构象控制来优化其蛋白质框架的动力学以实现有效的催化。虽然它是很难采用类似的策略，以提高催化合成酶，我们在这里报告，调制的活性位点的底物的动态是很容易实现的分子印迹纳米粒子（MINP）和它的酸辅因子之间的复合物，通过调整的大小和形状的印迹网站。随着烷基葡糖苷底物以增加的强度结合并保持在更紧密配合的口袋中，酸催化的聚糖水解变得更加困难。更大、更宽的活性位点，虽然不太能够结合底物，但提供更高的催化活性，这可能是由于对于一般的酸催化，底物和酸辅因子更容易对齐。底物选择性由糖苷配基结合位点的紧密性和聚糖结合硼氧杂环戊烯基团的取向控制。
Enzymes use sophisticated conformational control to optimize the dynamics of their protein framework for efficient catalysis. Although it is difficult to employ a similar strategy to improve catalysis in a synthetic enzyme, we here report that modulation of the dynamics of the substrate in the active site is readily achievable in a complex between a molecularly imprinted nanoparticle (MINP) and its acid cofactor, through tuning of the size and shape of the imprinted site. As the alkyl glucoside substrate is bound with increasing strength and held in a more tightly fitted pocket, the acid-catalyzed glycan hydrolysis becomes more difficult. A larger, wider active site, although less able to bind the substrate, affords a higher catalytic activity, likely due to easier alignment of the substrate and the acid cofactor for a general acid catalysis. The substrate selectivity is controlled by both the tightness of the aglycon-binding site and the orientation of the glycan-binding boroxole group.
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影响因子：
12.9
作者：
Li X;Zhao Y
通讯作者：
Zhao Y
影响因子：
56.9
作者：
KRAUT, J
通讯作者：
KRAUT, J
影响因子：
15
作者：
Kim, Hyunkyu;Kang, Young Ji;Kim, Kyoung Taek
通讯作者：
Kim, Kyoung Taek
影响因子：
1.8
作者：
Muratsugu, Satoshi;Shirai, Sora;Tada, Mizuki
通讯作者：
Tada, Mizuki
选择性识别水中单糖和低聚糖的通用方法。
影响因子：
15
作者：
Gunasekara RW;Zhao Y
通讯作者：
Zhao Y