Enzymes in organic syntheses. 19. Evaluation of the stereoselectivities of horse liver alcohol dehydrogenase; catalyzed oxidoreductions of hydroxy- and ketothiolanes, -thianes, and -thiepanes

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Abstract
The specificity of horse liver alcohol dehydrogenase (HLADH) with respect to unsubstituted five-, six-, and seven-membered ring 3- and 4-thiaketone and -thiaalcohol substrates has been examined. The enzyme is found to have a broad tolerance of the structural variations within this series. HLADH also exhibits encouraging (up to 46%) enantiotopic and enantiomeric specificity in preparative-scale reduction and oxidation reactions of the heterocyclic ketones and alcohols respectively.