动力学分辨率
紫红色杆菌
化学
基质(水族馆)
胺气处理
酶动力学
催化作用
对映选择合成
热稳定性
溶解度
组合化学
立体化学
有机化学
活动站点
生物化学
地质学
群体感应
海洋学
基因
毒力
作者
Cristian Andrei Gal,Laura Edit Barabás,Andrea Varga,Pál Csuka,László Csaba Bencze,Monica Ioana Toșa,László Poppe,Csaba Paizs
标识
DOI:10.1016/j.mcat.2022.112660
摘要
Amine transaminases (TAs) are attractive biocatalysts for the synthesis of chiral aromatic amines representing highly valuable motifs of APIs. The increased industrial need of novel methods to produce chiral amines for APIs resulted in an emerged discovery of new TAs. Joining the current wave of TA related research, this study reports the identification of genes encoding an (S)-selective TA from Pseudomonas psychrotolerans TA (PpS-TA) and an (R)-selective TA from Shinorizobium sp. TA (SrR-TA) by sequence data mining. Functional analysis of the novel TAs revealed their pH profile, thermal stability, optimal buffer system, DMSO tolerance, and operational stability in kinetic resolution (KR) of racemic 1-phenylethane-1-amines. The (S)-selective PpS-TA maintained its operational stability even at high temperature and pH values, enabling conversions from racemates approaching the optimal ∼50% value of a highly selective KR. Although with lower activity, the (R)-selective SrR-TA remained active at higher DMSO co-solvent concentrations up to 30%, enabling elevated substrate concentrations for aromatic amines of low water-solubility. The kinetic parameters of the novel PpS-TA and SrR-TA in KRs of several racemic 1-arylethane-1-amines (±)-2a-d and pyruvate (co-substrate) revealed superior catalytic efficiencies (kcat values) compared to the well-characterized (S)-TA from Chromobacterium violaceum (CvS-TA) indicating the biocatalytic potential of the two newly characterized TAs.
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