苏氨酸醛缩酶的催化机理、分子改造及合成应用  

Catalytic mechanism, molecular engineering and applications of threonine aldolases

作　　者：陈启佳 陈曦[2] 郝建雄[1] 朱敦明[2] Qijia Chen;Xi Chen;Jianxiong Hao;Dunming Zhu(College of Biological Science and Engineering,Hebei University of Science and Technology,Shijiazhuang 050018,Hebei,China;National Engineering Laboratory for Industrial Enzymes,Tianjin Institute of Industrial Biotechnology,Chinese Academy of Sciences,Tianjin 300308,China)

机构地区：[1]河北科技大学生物科学与工程学院,河北石家庄050018 [2]中国科学院天津工业生物技术研究所工业酶国家工程实验室,天津300308

出　　处：《生物工程学报》2021年第12期4215-4230,共16页Chinese Journal of Biotechnology

基　　金：国家自然科学基金(No.22001056);河北省自然科学基金(No.B2020208050)资助。

摘　　要：苏氨酸醛缩酶催化醛和甘氨酸羟醛缩合,一步反应即可构建产物β-羟基-α-氨基酸的两个手性中心,从原子经济性和环境影响角度,是非常具有潜力的绿色合成光学纯β-羟基-α-氨基酸的方式之一。多个不同生物来源的苏氨酸醛缩酶得到分离和表征,较低的β-碳立体选择性以及反应过程中动力学和热力学控制难题,使其在合成应用中面临很大挑战。文中综述了近年来苏氨酸醛缩酶在基因挖掘、催化机理、高通量筛选与分子改造、合成应用等方面的研究进展,旨在为进一步研究提供参考。Threonine aldolases catalyze the aldol condensation of aldehydes with glycine to furnish β-hydroxy-α-amino acid with two stereogenic centers in a single reaction. This is one of the most promising green methods for the synthesis of optically pure β-hydroxy-α-amino acid with high atomic economy and less negative environmental impact. Several threonine aldolases from different origins have been identified and characterized. The insufficient β-carbon stereoselectivity and the challenges of balancing kinetic versus thermodynamic control to achieve the optimal optical purity and yield hampered the application of threonine aldolases. This review summarizes the recent advances in discovery, catalytic mechanism,high-throughput screening, molecular engineering and applications of threonine aldolases, with the aim to provide some insights for further research in this field.

关 键 词：L-苏氨酸醛缩酶 D-苏氨酸醛缩酶 β-羟基-α-氨基酸 催化机理 分子改造 

分 类 号：TQ426.97[化学工程] TQ226.36