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1990•Journal of the Chemical Society Chemical CommunicationsRequires access

A new NAD-dependent alcohol dehydrogenase with opposite facial selectivity useful for asymmetric reduction and cofactor regeneration

Gwo‐Jenn Shen, Yi-Fong Wang, Curt W. Bradshaw, Chi‐Huey Wong

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Abstract

A new NAD-dependent alcohol dehydrogenase isolated from a Pseudomonas species catalysed the reduction of many acyclic ketones to optically active alcohols with very high enantioselectivity (90 to >98% enantiomeric excess); the stereochemical course of the reduction was determined to be the transfer of the pro-(R) hydrogen from NADH to the Si face of the carbonyl group, a process different from that for other known alcohol dehydrogenases.

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What this paper is about

A new NAD-dependent alcohol dehydrogenase isolated from a Pseudomonas species catalysed the reduction of many acyclic ketones to optically active alcohols with very high enantioselectivity (90 to >98% enantiomeric excess); the stereochemical course of the reduction was determined to be the transfer of the pro-(R) hydrogen from NADH to the Si face of the carbonyl group, a process different from that for other known alcohol dehydrogenases.

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OpenAlex reports 28 citations for this work. Citation counts describe recorded attention and do not establish research quality.

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Available abstract

A new NAD-dependent alcohol dehydrogenase isolated from a Pseudomonas species catalysed the reduction of many acyclic ketones to optically active alcohols with very high enantioselectivity (90 to >98% enantiomeric excess); the stereochemical course of the reduction was determined to be the transfer of the pro-(R) hydrogen from NADH to the Si face of the carbonyl group, a process different from that for other known alcohol dehydrogenases.

Key concepts: Alcohol dehydrogenase, Cofactor, NAD+ kinase, Chemistry, Alcohol, Enantiomer, Enantiomeric excess, Selectivity

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