169624-83-3Relevant academic research and scientific papers
Finding the Selectivity Switch - A Rational Approach towards Stereocomplementary Variants of the Ene Reductase YqjM
Rüthlein, Elisabeth,Classen, Thomas,Dobnikar, Lina,Sch?lzel, Melanie,Pietruszka, J?rg
, p. 1775 - 1786 (2015)
Ene reductases from the Old Yellow Enzyme family are versatile biocatalysts useful for the synthesis of optically active compounds. One disadvantage of biocatalysts when compared to competing catalysts in chemical syntheses is that often only one stereoisomer of the product is available. Another drawback can be the lack of activity in certain enzyme-substrate combinations. We were able to approach both of these challenges rationally in the case of the enzymatic synthesis of methyl 3-hydroxy-2-methylpropanoate (commonly denoted as the Roche ester) and derivatives thereof using the ene reductase YqjM. By a highly efficient, concept-based approach of designing mutant variants of YqjM and engineering substrates we could alter both the rate constant and the enantioselectivity of the reaction. Preparative scale reactions have been performed with successful mutants. In addition, the iterative modification of the substrate gave experiment-based insights into the binding mode of the Roche ester precursor and its derivatives.
The baker's yeast reduction of the β-keto aldehydes in the presence of a sulfur compound
Hayakawa, Ryuuichirou,Shimizu, Makoto
, p. 1298 - 1300 (2007/10/03)
Improved enantio- and diastereoselectivity was achieved in the baker's yeast reduction of β-keto aldehyde derivatives using a sulfur compound as an additive. The resulting enantiomerically pure diol was transformed into serricornin, a sex pheromone of the cigarette beetle.
