Variants of the Acyltransferase from Mycobacterium smegmatis Enable Enantioselective Acyl Transfer in Water,ACS Catalysis

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Variants of the Acyltransferase from Mycobacterium smegmatis Enable Enantioselective Acyl Transfer in Water
ACS Catalysis ( IF 11.3 ) Pub Date : 2020-08-17 , DOI: 10.1021/acscatal.0c02981
Etta Jost ₁ , Masoud Kazemi ₂ , Valerija Mrkonjić ₁ , Fahmi Himo ₂ , Christoph K. Winkler ₁ , Wolfgang Kroutil _{1,

3,

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Affiliation

The acyltransferase from Mycobacterium smegmatis (MsAcT) complements the well-established acylation activity of hydrolases in organic solvents with its activity to perform acylation reactions (among other reactions) in an aqueous environment. The enzyme’s potential is however limited, due to its poor regio- and stereoselectivity with enantioselectivities (E-values) below 20 for bulky (aromatic) substrates. By applying computer-guided rational design, a library of single variants was designed that allowed conversion of a set of previously challenging substrates with good activity and E-values up to >200. The computational predictions were found to be in agreement with experimental data, which in turn allowed for the generation of even more active and selective double variants. Overall, the produced set of variants provides a toolbox for the enantioselective acylation of challenging alcohols in water, effectively contributing to an alternative to reactions in organic solvents.

中文翻译：

来自耻垢分枝杆菌的酰基转移酶的变体能够在水中进行对映选择性酰基转移

耻垢分枝杆菌的酰基转移酶（MsAcT）补充了水解酶在有机溶剂中公认的酰化活性，并具有在水性环境中进行酰化反应（以及其他反应）的活性。然而，由于其对大的（芳香族）底物的对映选择性（E值）低于20，由于其区域和立体选择性差，该酶的潜力受到限制。通过应用计算机指导的合理设计，设计了一个单一变异体的库，该库允许转换一组具有良好活性且E值高达> 200的先前具有挑战性的底物。发现计算预测与实验数据一致，这反过来又允许生成更活跃和选择性的双变异体。总体，

更新日期：2020-09-20

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