Jürgen Heidlas

TL;DR: The NADPH-linked diacetyl reductase system from the cytosolic fraction of Saccharomyces cerevisiae has been resolved into two oxidoreductases catalyzing irreversibly the enantioselective reduction of diacety (2,3-butanedione) to (S)- and (R)-acetoin (3-hydroxy-2-butanone) which have been isolated to apparent electrophoretical purity.

TL;DR: Two NADPH-dependent oxidoreductases catalyzing the enantioselective reduction of 3-oxo esters to (S)- and (R)-3-hydroxy acid esters have been purified 121- and 332-fold from cell extracts of Saccharomyces cerevisiae.

TL;DR: A NAD-dependent (R)-2,3-butanediol dehydrogenase, isolated from cell extracts of the yeast Saccharomyces cerevisiae, was capable to reduce irreversibly diacetyl (2, 3- butanediol) to (R)acetoin (3-hydroxy-2-butanone) and in a subsequent reaction reversibly to

TL;DR: Results imply that the moderate optical purities of alkan-2-ols obtained by the reduction of methylketones employing intact yeast cells are not due to a partial enantioselectivity of YADH, but the stereochemical outcome of in vivo reductions cannot be exclusively explained by the additional action of (S)-DR.