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: A slightly different result was obtained by applying 3-methylcyclohex-2-en-1-ol (4a) to the sequential enzyme cascade. In this particular biotransformation each step turned out to be highly selective with respect to all different substrates and stereochemistry (Fig. 2). The alcohol oxidation of (4a) to the corresponding enone (4b) was rather slow, and intermediate (4b) was not accepted by the enoate reductase NemR at all. After addition of OYE1 saturated ketone (4c) was obtained in about 20% yield whereas no reduction to the corresponding saturated 3-methylcyclohexanol was observed. In the final step the Baeyer–Villiger monooxygenase CHMOAcineto converted (4c) in 82% overall yield toward (4d) with perfect regio- and enantioselectivity (>99% distal lactone, 99% ee).
Affiliation: Institute of Applied Synthetic Chemistry, Vienna University of Technology, Getreidemarkt 9/163-OC, 1060 Vienna, Austria.