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Two‐Enzyme Hydrogen‐Borrowing Amination of Alcohols Enabled by a Cofactor‐Switched Alcohol Dehydrogenase
Author(s) -
Thompson Matthew P.,
Turner Nicholas J.
Publication year - 2017
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201701092
Subject(s) - cofactor , alcohol dehydrogenase , chemistry , reductive amination , amination , nad+ kinase , substrate (aquarium) , enzyme , amine gas treating , alcohol , combinatorial chemistry , dehydrogenase , biocatalysis , catalysis , stereochemistry , biochemistry , organic chemistry , reaction mechanism , biology , ecology
The NADPH‐dependent secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus (TeSADH), displaying broad substrate specificity and low enantioselectivity, was engineered to accept NADH as a cofactor. The engineered TeSADH showed a >10 000‐fold switch from NADPH towards NADH compared to the wildtype enzyme. This TeSADH variant was applied to a biocatalytic hydrogen‐borrowing system that employed catalytic amounts of NAD + , ammonia, and an amine dehydrogenase, which thereby enabled the conversion a range of alcohols into chiral amines.