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: Consequently, the non-sequential in vitro transformations were compared to our recently published in vivo approach (Oberleitner et al., 2013). Fig. 5 displays a comparative study between the in vitro and in vivo cascade of 3-methylcyclohex-2-en-1-ol (4a). The overall reaction performances were highly similar, but a faster transformation was observed in vitro.
Affiliation: Institute of Applied Synthetic Chemistry, Vienna University of Technology, Getreidemarkt 9/163-OC, 1060 Vienna, Austria.