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

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...

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Veröffentlicht in:	ChemCatChem 2017-10, Vol.9 (20), p.3833-3836
Hauptverfasser:	Thompson, Matthew P., Turner, Nicholas J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Alcohol Alcohol dehydrogenase Alcohols amination Amines Ammonia biocatalysis Catalysis Dehydrogenases Enzymes hydrogen borrowing Nicotinamide adenine dinucleotide protein engineering
Online-Zugang:	Volltext
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