Recent advances in imine reductase-catalyzed reactions

被引:58
|
作者
Lenz, Maike [1 ]
Borlinghaus, Niels [1 ]
Weinmann, Leonie [1 ]
Nestl, Bettina M. [1 ]
机构
[1] Univ Stuttgart, Inst Biochem & Tech Biochem, Allmandring 31, D-70569 Stuttgart, Germany
来源
关键词
Imine reductases; Reductive amination; Cofactor specificity; Engineering; Cascade reaction; N-Heterocycles; OPTICALLY-ACTIVE AMINES; COFACTOR-REGENERATION; ASYMMETRIC REDUCTION; (R)-IMINE REDUCTASE; SELECTIVE REDUCTION; ENZYME PROMISCUITY; ACID OXIDASE; AMINATION; DEHYDROGENASE; TOOLBOX;
D O I
10.1007/s11274-017-2365-8
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
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.
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页数:10
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