鉴定一种用于还原大位阻二氢异喹啉的亚胺还原酶。
Identification of an Imine Reductase for Asymmetric Reduction of Bulky Dihydroisoquinolines.
机构信息
State Key Laboratory of Bioreactor Engineering, Shanghai Collaborative Innovation Center for Biomanufacturing, East China University of Science and Technology , 130 Meilong Road, Shanghai 200237, P. R. China.
Shanghai Institute of Organic Chemistry, Chinese Academy of Science , 345 Lingling Road, Shanghai 200032, P. R. China.
出版信息
Org Lett. 2017 Jun 16;19(12):3151-3154. doi: 10.1021/acs.orglett.7b01274. Epub 2017 Jun 8.
A new imine reductase from Stackebrandtia nassauensis (SnIR) was identified, which displayed over 25- to 1400-fold greater catalytic efficiency for 1-methyl-3,4-dihydroisoquinoline (1-Me DHIQ) compared to other imine reductases reported. Subsequently, an efficient SnIR-catalyzed process was developed by simply optimizing the amount of cosolvent, and up to 15 g L 1-Me DHIQ was converted completely without a feeding strategy. Furthermore, the reaction proceeded well for a panel of dihydroisoquinolines, affording the corresponding tetrahydroisoquinolines (mostly in S-configuration) in good yields (up to 81%) and with moderate to excellent enantioselectivities (up to 99% ee).
从斯塔克氏菌属（Stackebrandtia）nassauensis 中鉴定出一种新型亚胺还原酶（SnIR），与已报道的其他亚胺还原酶相比，该酶对 1-甲基-3,4-二氢异喹啉（1-Me DHIQ）的催化效率高出 25-1400 倍。随后，通过简单优化共溶剂的用量，开发了一种高效的 SnIR 催化工艺，在没有进料策略的情况下，高达 15 g/L 的 1-Me DHIQ 被完全转化。此外，该反应对一系列二氢异喹啉都能很好地进行，以中等至优异的对映选择性（高达 99%ee）获得相应的四氢异喹啉（主要为 S-构型），收率良好（高达 81%）。
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