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

Matthew P. Thompson; Nicholas J. Turner

doi:10.1002/cctc.201701092

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

Matthew P. Thompson, Nicholas J. Turner^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Pages (from-to)	3833-3836
Number of pages	4
Journal	ChemCatChem
Volume	9
Issue number	20
Early online date	7 Jul 2017
DOIs	https://doi.org/10.1002/cctc.201701092
Publication status	Published - 2017

Keywords

amination
biocatalysis
enzymes
hydrogen borrowing
protein engineering

Research Beacons, Institutes and Platforms

Manchester Institute of Biotechnology

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10.1002/cctc.201701092

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title = "Two-Enzyme Hydrogen-Borrowing Amination of Alcohols Enabled by a Cofactor-Switched Alcohol Dehydrogenase",

abstract = "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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author = "Thompson, {Matthew P.} and Turner, {Nicholas J.}",

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AB - 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.

KW - amination

KW - biocatalysis

KW - enzymes

KW - hydrogen borrowing

KW - protein engineering

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

Abstract

Keywords

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