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.
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%）。
