Two‐Enzyme Hydrogen‐Borrowing Amination of Alcohols Enabled by a Cofactor‐Switched Alcohol Dehydrogenase | Zendy

Thompson Matthew P. | Zendy; Turner Nicholas J. | Zendy

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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.

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