Lenz Maike, Borlinghaus Niels, Weinmann Leonie, Nestl Bettina M
Institute of Biochemistry and Technical Biochemistry, Universitaet Stuttgart, Allmandring 31, 70569, Stuttgart, Germany.
World J Microbiol Biotechnol. 2017 Oct 11;33(11):199. doi: 10.1007/s11274-017-2365-8.
Imine reductases are nicotinamide-dependent enzymes that catalyze the asymmetric reduction of various imines to the corresponding amine products. Owing to the increasing roles of chiral amines and heterocyclic compounds as intermediates for pharmaceuticals, the demand for novel selective synthesis strategies is vitally important. Recent studies have demonstrated the discovery and structural characterization of a number of stereoselective imine reductase enzymes. Here, we highlight recent progress in applying imine reductases for the formation of chiral amines and heterocycles. It particularly focuses on the utilization of imine reductases in reductive aminations of aldehydes and ketones with various amine nucleophiles, one of the most powerful reactions in the synthesis of chiral amines. Second, we report on the synthesis of saturated substituted N-heterocycles by combining them with further biocatalysts, such as carboxylic acid reductases, oxidases or transaminases. Finally, we summarize the latest applications of imine reductases in the promiscuous asymmetric hydrogenation of a highly reactive carbonyl compound and the engineering of the cofactor specificity from NADPH to NADH.
亚胺还原酶是依赖烟酰胺的酶，可催化各种亚胺不对称还原为相应的胺产物。由于手性胺和杂环化合物作为药物中间体的作用日益增加，对新型选择性合成策略的需求至关重要。最近的研究已经证明了多种立体选择性亚胺还原酶的发现和结构表征。在此，我们重点介绍应用亚胺还原酶形成手性胺和杂环的最新进展。它特别关注亚胺还原酶在醛和酮与各种胺亲核试剂的还原胺化反应中的应用，这是手性胺合成中最强大的反应之一。其次，我们报告了通过将它们与其他生物催化剂（如羧酸还原酶、氧化酶或转氨酶）结合来合成饱和取代的N-杂环化合物。最后，我们总结了亚胺还原酶在高活性羰基化合物的混杂不对称氢化以及辅因子特异性从NADPH工程改造为NADH方面的最新应用。
