MSRA公司
动力学分辨率
化学
亚砜
蛋氨酸亚砜还原酶
对映选择合成
立体化学
生物催化
基质(水族馆)
合理设计
组合化学
有机化学
催化作用
生物化学
氨基酸
蛋氨酸
反应机理
海洋学
地质学
生物
遗传学
作者
Silvia Anselmi,Alexandra Carvalho,Angela Serrano-Sanchez,Jose‐Luis Ortega Roldan,Jill Caswell,Iman Omar,Gustavo Perez-Ortiz,Sarah M. Barry,Thomas S. Moody,Daniele Castagnolo
标识
DOI:10.1021/acscatal.3c00372
摘要
Methionine sulfoxide reductase A (MsrA) enzymes have recently found applications as nonoxidative biocatalysts in the enantioselective kinetic resolution of racemic sulfoxides. This work describes the identification of selective and robust MsrA biocatalysts able to catalyze the enantioselective reduction of a variety of aromatic and aliphatic chiral sulfoxides at 8-64 mM concentration with high yields and excellent ees (up to 99%). Moreover, with the aim to expand the substrate scope of MsrA biocatalysts, a library of mutant enzymes has been designed via rational mutagenesis utilizing in silico docking, molecular dynamics, and structural nuclear magnetic resonance (NMR) studies. The mutant enzyme MsrA33 was found to catalyze the kinetic resolution of bulky sulfoxide substrates bearing non-methyl substituents on the sulfur atom with ees up to 99%, overcoming a significant limitation of the currently available MsrA biocatalysts.
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