Enzymes in organic syntheses. 19. Evaluation of the stereoselectivities of horse liver alcohol dehydrogenase; catalyzed oxidoreductions of hydroxy- and ketothiolanes, -thianes, and -thiepanes
- 1 June 1981
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Chemistry
- Vol. 59 (11), 1574-1579
- https://doi.org/10.1139/v81-232
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.This publication has 4 references indexed in Scilit:
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- Enzymes in organic synthesis. Influence of substrate structure on rates of horse liver alcohol dehydrogenase-catalysed oxidoreductionsJournal of the Chemical Society, Perkin Transactions 1, 1978