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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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Comparison of in vitro and in vivo results of 3-methyl-2-cyclohexen-1-ol cascade of LK-ADH, OYE1 and CHMOAcineto.
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fig0040: Comparison of in vitro and in vivo results of 3-methyl-2-cyclohexen-1-ol cascade of LK-ADH, OYE1 and CHMOAcineto.

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.


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)

Comparison of in vitro and in vivo results of 3-methyl-2-cyclohexen-1-ol cascade of LK-ADH, OYE1 and CHMOAcineto.
© Copyright Policy - CC BY-NC-ND
Related In: Results  -  Collection

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

fig0040: Comparison of in vitro and in vivo results of 3-methyl-2-cyclohexen-1-ol cascade of LK-ADH, OYE1 and CHMOAcineto.
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.

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