Recent advances in the biocatalytic reduction of ketones and oxidation of sec-alcohols.
To improve the efficiency and applicability of biocatalytic redox-reactions for asymmetric ketone-reduction and enantioselective alcohol-oxidation catalyzed by nicotinamide-dependent dehydrogenases/reductases, several achievements for cofactor-recycling have been made during the last two years. First, the use of hydrogenases for NADPH recycling in a two enzyme system. Second, preparative transformations with alcohol dehydrogenases coupled with NADH oxidases for NAD+/NADP+ recycling. Third, an exceptional chemo-stable alcohol dehydrogenase can efficiently use i-propanol and acetone as cosubstrates for reduction and oxidation, respectively, in a single-enzyme system. Novel carbonyl reductases and dehydrogenases derived from plant cells are particularly suited for sterically demanding substrates.
Kroutil
Wolfgang
W
Department of Chemistry, Organic and Bioorganic Chemistry, University of Graz, Austria.
Mang
Harald
H
Edegger
Klaus
K
Faber
Kurt
K
D000438:Alcohols / Q000737:chemistry / Q000378:metabolism*; D001419:Bacteria / Q000201:enzymology; D001711:Biotransformation; D002384:Catalysis; D007659:Ketones / Q000737:chemistry / Q000378:metabolism*; D015394:Molecular Structure; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry / Q000378:metabolism
D000438:Alcohols; D007659:Ketones; D010088:Oxidoreductases