转氨作用
脱氨基
基质(水族馆)
丙氨酸
化学
动力学分辨率
对映体药物
产量(工程)
转氨酶
氨基酸
对映选择合成
胺气处理
胺化
催化作用
立体化学
有机化学
酶
生物化学
材料科学
冶金
地质学
海洋学
作者
Jianjiong Li,Shanshan Yu,Y.G. Wang,Peiyuan Yao,Qiaqing Wu,Dunming Zhu
标识
DOI:10.1021/acs.oprd.1c00408
摘要
(S)-2-Aminobutane, d-alanine, and d-homoalanine are important intermediates for the production of various active pharmaceutical ingredients and food additives. The preparation of these small chiral amine or amino acids with high water solubility still demands searching for efficient methods. In this work, we identified an ω-transaminase (ω-TA) from Sinirhodobacter hungdaonensis (ShdTA) that catalyzed the kinetic resolution of racemic 2-aminobutane at a concentration of 800 mM using pyruvate as the amino acceptor, leading to the simultaneous isolation of enantiopure (S)-2-aminobutane and d-alanine in 46% and 90% yield, respectively. In addition, (S)-2-aminobutane (98% ee) and d-homoalanine (99% ee) were isolated in 45% and 93% yield, respectively, in the kinetic resolution of racemic 2-aminobutane at a concentration of 400 mM coupled with deamination of l-threonine by threonine deaminase. We thus developed a biocatalytic process for the practical synthesis of these valuable small chiral amine and d-amino acids.
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