Enzymatic Biosynthesis of l-2-Aminobutyric Acid by Glutamate Mutase Coupled with l-Aspartate-β-decarboxylase Using l-Glutamate as the Sole Substrate,ACS Catalysis

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Enzymatic Biosynthesis of l-2-Aminobutyric Acid by Glutamate Mutase Coupled with l-Aspartate-β-decarboxylase Using l-Glutamate as the Sole Substrate
ACS Catalysis ( IF 11.3 ) Pub Date : 2020-11-16 , DOI: 10.1021/acscatal.0c04141
Yufeng Liu ₁ , Laichuang Han ₁ , Zhongyi Cheng ₁ , Zhongmei Liu ₁ , Zhemin Zhou ₁

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l-2-Aminobutyric acid (L-ABA) is a chiral precursor of several important drugs. l-Glutamate is an ideal material for the production of L-ABA through γ-decarboxylation; however, enzyme-mediated γ-decarboxylation of l-glutamate has not yet been reported. Here, this goal was achieved through isomerization of l-glutamate to (2S,3S)-3-methylaspartate by glutamate mutase (GM) and β-decarboxylation of 3-methylaspartate by l-aspartate-β-decarboxylase (Asd). Although the activity of wild-type Asd toward 3-methylaspartate could not be detected, a mutant Asd exhibiting high activity was isolated on the basis of enzyme engineering. The conversion of l-glutamate to L-ABA achieved 98.9%, which provided a more cost-effective process for L-ABA industrial production.

中文翻译：

以谷氨酸为唯一底物的谷氨酸突变酶与l-天冬氨酸-β-脱羧酶偶联酶生l-2-氨基丁酸

l -2-氨基丁酸（L-ABA）是几种重要药物的手性前体。l-谷氨酸盐是通过γ-脱羧生产L-ABA的理想材料；然而，尚未报道酶介导的1-谷氨酸的γ-脱羧。在此，通过谷氨酸突变酶（GM）将1-谷氨酸异构化为（2 S，3 S）-3-甲基天冬氨酸，并通过1-天冬氨酸-β-脱羧酶（Asd）将3-甲基天冬氨酸β-脱羧实现了该目标。尽管不能检测到野生型Asd对3-甲基天冬氨酸的活性，但是基于酶工程分离了具有高活性的突变体Asd。l的转换谷氨酸转化为L-ABA的比例达到98.9％，这为L-ABA工业生产提供了更具成本效益的工艺。

更新日期：2020-12-04

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