ω-转氨酶分子改造研究进展.PDFVIP

生 物 工 程 学 报 高新星 等/-转氨酶分子改造研究进展 1057 Chinese Journal of Biotechnology /cjbcn Jul. 25, 2018, 34(7): 1057−1068 DOI: 10.13345/j.cjb.170455 ©2018 Chin J Biotech, All rights reserved ·综 述· - 高新星，韦平和 225300 , . -. , 2018, 34(7): 1057–1068. Gao XX, Wei PH. Advances in molecular modification of -transaminase. Chin J Biotech, 2018, 34(7): 1057–1068. 摘 要 : -转氨酶能催化羰基化合物发生不对称还原胺化反应，在制备手性胺类化合物方面具有较好的应用前 景。由于底物结合区域特殊的空间结构，野生型 -转氨酶在合成大位阻手性胺方面的应用受到了限制。此外， 在立体选择性和稳定性方面这一类酶也存在一些不足，目前满足工业应用需求的 -转氨酶仍较为有限。文中首 先介绍了-转氨酶的结构特征和催化机制，并探讨S 型和R 型酶在结构特征方面的主要差异。然后对-转氨酶 的分子改造研究进行了综述，重点阐述了基于结构特征和催化机制进行的分子改造研究，包括底物特异性改造、 立体选择性改造和稳定性改造三方面。最后，对-转氨酶分子改造研究进展进行总结和展望。 : -转氨酶，结构，分子改造，底物特异性，稳定性 Advances in molecular modification of -transaminase Xinxing Gao, and Pinghe Wei Jiangsu Key Laboratory of Chiral Pharmaceuticals Biosynthesis, College of Pharmacy and Chemistry and Chemical Engineering, Taizhou University, Taizhou 225300, Jiangsu, China Abstract: -Transaminase catalyzes the asymmetric reductive amination of carbonyl compounds, and has great application prospect in the preparation of chiral amines. The application in synthesis of bulky chiral amines is limited by the special structure of substrate binding region in the wild-type enzyme. Moreover, there are also some drawbacks in the stereoselectivity and stability of -transaminase. So far, -transaminase satisfying the industrial requirements is still rare. In this review, we first introduce the structure and catalytic mechanism of -transaminase, and then discuss the structural differences between S-selective and R-selective enzymes. Molecular modification of -tra