ChemCatChem
ChemCatChem
4 years ago

Two-Enzyme Hydrogen-Borrowing Amination of Alcohols Enabled by a Cofactor-Switched Alcohol Dehydrogenase

Two-Enzyme Hydrogen-Borrowing Amination of Alcohols Enabled by a Cofactor-Switched Alcohol Dehydrogenase
Matthew P. Thompson, Nicholas J. Turner
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. Designed to share: Rational engineering of the cofactor dependence in a nonselective alcohol dehydrogenase opens the door to a second generation of hydrogen-borrowing enzyme cascades for the amination of alcohols.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/cctc.201701092

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