Abstract
In our effort to search for carbonyl reductases with anti-Prelog enantioselectivity, the activity and enantioselectivity of a carbonyl reductase from Candida magnoliae have been examined with various ketones of diverse structures. This carbonyl reductase catalyzed the reduction of a series of ketones, alpha- and beta-ketoesters, to anti-Prelog configurated alcohols in excellent optical purity. The usefulness of this carbonyl reductase has been demonstrated by synthesis of several chiral alcohol intermediates of pharmaceutical importance.
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