NADH-dependent ketone reductase

An NADH-dependent reductase (ScCR) was identified by genome mining studies of Streptomyces coelicolor. This dehydrogenase showed broad tolerance to pro-chiral ketones including aryl ketones, a- and 3-ketoesters and had particularly high activity and excellent enantioselectivity (>99% ee) for the last substrate type For example the enzyme reduced ethyl 4-chloro-3-oxobutanoate (CORE)... 

Diverse soluble enzymes, called aldo-keto reductases. cany out bioreduction of aldehydes and ketones. They are found in the liver and other tissues (e.g.. kidney). As a general class, these soluble en7.ynie.s have similar physi-ochemical properties and broad substrate specificities and require NADW as a cofactor. Oxidoreductase enzymes that catty out both oxidation and reduction reactions also can reduce aldehydes and ketones. " For example. Ihe important liver alcohol dehydrogenase is an NAD -dependent oxido-icductase that oxidizes ethanol and other aliphatic alcohols to aldehydes and ketones. In the presence of NADH or... 

Enoate reductases (EC 1.3.1.31) are flavin-dependent and iron-sulfur-contain-ing proteins found among others in Clostridium species. Members of this NADHrflavin oxidoreductase/NADH oxidase family are distinguished from other ERs due to their high stereospecificity and strict regioselectivity for the reduction of double bonds of monoacids and monoesters, as well as reducing classical substrates such as a,p-unsaturated aldehydes, cyclic ketones, and methyl ketones. However, these enzymes are extremely oxygen sensitive, so they have not been employed in biocatalysis so far [2,3]. 

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