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In vitro characterization of an enzymatic redox cascade composed of an alcohol dehydrogenase, an enoate reductases and a Baeyer-Villiger monooxygenase.

Oberleitner N, Peters C, Rudroff F, Bornscheuer UT, Mihovilovic MD - J. Biotechnol. (2014)

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.

View Article: PubMed Central - PubMed

Affiliation: Institute of Applied Synthetic Chemistry, Vienna University of Technology, Getreidemarkt 9/163-OC, 1060 Vienna, Austria.

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Sequential in vitro cascade starting from cyclohexen-2-ol (1a).
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fig0020: Sequential in vitro cascade starting from cyclohexen-2-ol (1a).

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).


In vitro characterization of an enzymatic redox cascade composed of an alcohol dehydrogenase, an enoate reductases and a Baeyer-Villiger monooxygenase.

Oberleitner N, Peters C, Rudroff F, Bornscheuer UT, Mihovilovic MD - J. Biotechnol. (2014)

Sequential in vitro cascade starting from cyclohexen-2-ol (1a).
© Copyright Policy - CC BY-NC-ND
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4263279&req=5

fig0020: Sequential in vitro cascade starting from cyclohexen-2-ol (1a).
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).

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.

View Article: PubMed Central - PubMed

Affiliation: Institute of Applied Synthetic Chemistry, Vienna University of Technology, Getreidemarkt 9/163-OC, 1060 Vienna, Austria.

Show MeSH