In vitro characterization of an enzymatic redox cascade composed of an alcohol dehydrogenase, an enoate reductases and a Baeyer-Villiger monooxygenase.
Bottom Line: An artificial enzyme cascade composed of an alcohol dehydrogenase, an enoate reductase and a Baeyer-Villiger monooxygenase was investigated in vitro to gain deeper mechanistic insights and understand the assets and drawbacks of this multi-step biocatalysis.Several substrates composed of different structural motifs were examined and provided access to functionalized chiral compounds in high yields (up to >99%) and optical purities (up to >99%).Hence, the applicability of the presented enzymatic cascade was exploited for the synthesis of biorenewable polyesters.
Affiliation: Institute of Applied Synthetic Chemistry, Vienna University of Technology, Getreidemarkt 9/163-OC, 1060 Vienna, Austria.Show MeSH
Mentions: We started our investigations to gain a better understanding of the presented redox cascade by characterizing each individual reaction and several different substrates (Scheme 2). In a first attempt we performed a sequential approach by adding all enzymes and their appropriate cofactors after defined time intervals. Our model reaction (Fig. 1) was the transformation of 2-cyclohexen-1-ol (1a) to the corresponding ɛ-caprolactone (1d).
Affiliation: Institute of Applied Synthetic Chemistry, Vienna University of Technology, Getreidemarkt 9/163-OC, 1060 Vienna, Austria.