Identification of an Imine Reductase for Asymmetric Reduction of Bulky Dihydroisoquinolines

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 develop...

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Published inOrganic letters Vol. 19; no. 12; pp. 3151 - 3154
Main Authors Li, Hao, Tian, Ping, Xu, Jian-He, Zheng, Gao-Wei
Format Journal Article
LanguageEnglish
Published WASHINGTON American Chemical Society 16.06.2017
Amer Chemical Soc
Subjects
catalytic activity
chemical reactions
chemical structure
Chemistry
Chemistry, Organic
feeding methods
imines
Physical Sciences
Science & Technology
tetrahydroisoquinolines
AMINATION
OVERACTIVE BLADDER
PAENIBACILLUS-LACTIS
TRANSFER HYDROGENATION
(S)-IMINE REDUCTASE
SELECTIVE REDUCTION
BIOTIN-STREPTAVIDIN TECHNOLOGY
(R)-IMINE REDUCTASE
CYCLIC IMINES
HIGHLY EFFICIENT
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Summary: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 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).
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ISSN:1523-7060
1523-7052
1523-7052
DOI:10.1021/acs.orglett.7b01274