Abstract
Microbes have an enormous diversity of alcohol and aldehyde oxidoreductases. A brief overview is given of the types known and of some novel ones discovered recently. Except from the classical, NAD-dependent, alcohol dehydrogenase (the long chain, zinc-containing type, EC 1.1.1.1), these enzymes are unexplored with respect to enantioselectivity. The present paper shows that quinohaemoprotein ethanol dehydrogenases, enzymes containing PQQ and haem c as cofactors and occurring in bacteria having very efficient respiratory chains for ethanol oxidation (e.g. Acetic acid bacteria), are well suited for the kinetic resolution of racemic alcohols (the C3 -synthons glycidol and solketal). Methods are dicussed to measure reliable E-values (enantiomeric ratio) of the enzymes with respect to substrate and intermediates. For that purpose, methods based on initial rate kinetics and end point determinations as well as progression curve analysis were applied. Some preliminary results on the effect of cofactor engineering on enantioselectivity indicate that changes in negative as well as positive sense can be expected.
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Geerlof, A., Van Tol, J.B.A., Jongejan, J.A., Duine, J.A. (1992). Microbial Alcohol/Aldehyde Oxidoreductases in Enantioselective Conversions. In: Servi, S. (eds) Microbial Reagents in Organic Synthesis. NATO ASI Series, vol 381. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-2444-7_33
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DOI: https://doi.org/10.1007/978-94-011-2444-7_33
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