Mathew Sam, Nadarajan Saravanan Prabhu, Sundaramoorthy Uthayasuriya, Jeon Hyunwoo, Chung Taeowan, Yun Hyungdon
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, The Netherlands.
Department of Bioscience and Biotechnology, Konkuk University, Seoul, 05029, Korea.
Biotechnol Lett. 2017 Apr;39(4):535-543. doi: 10.1007/s10529-016-2271-4. Epub 2016 Dec 21.
To enzymatically synthesize enantiomerically pure β-amino acids from β-keto nitriles using nitrilase and ω-transaminase.
An enzyme cascade system was designed where in β-keto nitriles are initially hydrolyzed to β-keto acids using nitrilase from Bradyrhizobium japonicum and subsequently β-keto acids were converted to β-amino acids using ω-transaminases. Five different ω-transaminases were tested for this cascade reaction, To enhance the yields of β-amino acids, the concentrations of nitrilase and amino donor were optimized. Using this enzymatic reaction, enantiomerically pure (S)-β-amino acids (ee > 99%) were generated. As nitrilase is the bottleneck in this reaction, molecular docking analysis was carried out to depict the poor affinity of nitrilase towards β-keto acids.
A novel enzymatic route to generate enantiomerically pure aromatic (S)-β-amino acids from β-keto nitriles is demonstrated for the first time.
使用腈水解酶和ω-转氨酶从β-酮腈酶促合成对映体纯的β-氨基酸。
设计了一种酶级联系统，其中首先使用来自日本慢生根瘤菌的腈水解酶将β-酮腈水解为β-酮酸，随后使用ω-转氨酶将β-酮酸转化为β-氨基酸。对五种不同的ω-转氨酶进行了该级联反应测试，为提高β-氨基酸的产率，对腈水解酶和氨基供体的浓度进行了优化。通过这种酶促反应，生成了对映体纯的（S）-β-氨基酸（对映体过量>99%）。由于腈水解酶是该反应的瓶颈，进行了分子对接分析以描述腈水解酶对β-酮酸的低亲和力。
首次展示了一种从β-酮腈生成对映体纯的芳香族（S）-β-氨基酸的新型酶促途径。
