There is a group of reductases that catalyze the reduction of various aldehydes and ketones (1,2). They occur widely in living organisms and are suggested to be involved in the metabolism of biogenic and xenobiotic carbonyl compounds. From the viewpoint of the practical application of these reductases, the stereospecific reduction of carbonyl compounds with enzymes exhibiting stereospecificity is an effective method for the production of various optically active alcohols (3-6).
Among these enzymes catalyzing the reduction of various carbonyl compounds, a class of monomeric NADPH-dependent oxidoreductases with molecular masses of about 35 kDa, called the aldo-keto reductase superfamily (7), has been well characterized. This superfamily contains many reductases, such as aldehyde reductase (EC 188.8.131.52), aldose reductase (EC 184.108.40.206), and so forth, and these proteins show high similarity in their substrate specificities and primary amino acid sequences (7). Here we describe aldehyde reductase and the application of microbial aldehyde reductase to the production of chiral alcohols.
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