Engineering Leifsonia Alcohol Dehydrogenase for Thermostability and Catalytic Efficiency by Enhancing Subunit Interactions,ChemBioChem

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Engineering Leifsonia Alcohol Dehydrogenase for Thermostability and Catalytic Efficiency by Enhancing Subunit Interactions
ChemBioChem ( IF 3.2 ) Pub Date : 2021-09-22 , DOI: 10.1002/cbic.202100431
Lu Zhu _{1,

2} , Yang Song _{3,

4} , Chenchen Chang _{3,

4} , Hongmin Ma ₂ , Lu Yang ₁ , Zixin Deng ₁ , Wei Deng _{3,

4} , Xudong Qu _{1,

2}

Affiliation

Engineering the subunit interface of Leifsonia alcohol dehydrogenase (LnADH) yielded thermostability, and catalytic efficiency significantly improved in the mutant T100R/S148I. T100R/S148I can efficiently convert various ketone substrates into nearly optically pure chiral alcohols at elevated temperature in a very low enzyme-to-substrate ratio (1 : 500).

中文翻译：

通过增强亚基相互作用来工程化 Leifsonia 酒精脱氢酶以提高热稳定性和催化效率

对Leifsonia醇脱氢酶 (LnADH)的亚基界面进行工程改造后，突变体 T100R/S148I 的热稳定性和催化效率显着提高。T100R/S148I 可以在高温下以非常低的酶与底物比 (1:500) 有效地将各种酮底物转化为几乎光学纯的手性醇。

更新日期：2021-11-16

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