Controlling Substrate Specificity and Stereospecificity of Alcohol Dehydrogenases

The ability to control the substrate specificity and stereochemistry of enzymatic reactions is of increasing interest in biocatalysis. As this review highlights, this control can be achieved through various means, including mutagenesis of active site residues and alteration of physical variables such as temperature and pressure as well as through changing the reaction medium. Although the focus of this article is on alcohol dehydrogenase reactions, each of these techniques can be readily applied toward other enzyme classes, as well.