A light-driven enzyme cascade reaction for the synthesis of lactones

Hanna Christiane Büchsenschütz; Fabian Schultes; S Schmidt; Robert Kourist

A light-driven enzyme cascade reaction for the synthesis of lactones

Hanna Christiane Büchsenschütz, Fabian Schultes, S Schmidt, Robert Kourist

Institute of Molecular Biotechnology (6550)

Research output: Contribution to conference › Poster

Abstract

Photosynthesis in the cyanobacterium Synechocystis sp. PCC 6803 is used to generate enough NADPH to drive the enzymatic reduction of cyclic ketones to their corresponding lactones. This reaction is catalyzed by the cyclohexanone monooxygenase (CHMO) from Acinetobacter calcoaceticus NCIMB 9871[1]. However, the reduction of saturated cyclic ketones by native alcoholdehydrogenases (ADHs) in Synechocysits sp. lower conversion rates. Minimized ketone concentrations and accelerated reactions toward the lactone would decrease the influence of ketoreduction. Here, the CHMO is combined with the ene-reductase YqjM of Bacillus subtilis in an cascade reaction. For now, both enzymes are expressed in different cells which were mixed for in vivo biotransformations. This offers the possibility to compensate expression levels and enzyme activities by precisely dosing both cells. However, coexpression of both enzymes would simplify the work progress and would prevent transport problems between the cells.

Original language	English
Publication status	Published - 9 Apr 2018

Cite this

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title = "A light-driven enzyme cascade reaction for the synthesis of lactones",

abstract = "Photosynthesis in the cyanobacterium Synechocystis sp. PCC 6803 is used to generate enough NADPH to drive the enzymatic reduction of cyclic ketones to their corresponding lactones. This reaction is catalyzed by the cyclohexanone monooxygenase (CHMO) from Acinetobacter calcoaceticus NCIMB 9871[1]. However, the reduction of saturated cyclic ketones by native alcoholdehydrogenases (ADHs) in Synechocysits sp. lower conversion rates. Minimized ketone concentrations and accelerated reactions toward the lactone would decrease the influence of ketoreduction. Here, the CHMO is combined with the ene-reductase YqjM of Bacillus subtilis in an cascade reaction. For now, both enzymes are expressed in different cells which were mixed for in vivo biotransformations. This offers the possibility to compensate expression levels and enzyme activities by precisely dosing both cells. However, coexpression of both enzymes would simplify the work progress and would prevent transport problems between the cells. ",

author = "B{\"u}chsensch{\"u}tz, {Hanna Christiane} and Fabian Schultes and S Schmidt and Robert Kourist",

year = "2018",

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TY - CONF

T1 - A light-driven enzyme cascade reaction for the synthesis of lactones

AU - Büchsenschütz, Hanna Christiane

AU - Schultes, Fabian

AU - Schmidt, S

AU - Kourist, Robert

PY - 2018/4/9

Y1 - 2018/4/9

N2 - Photosynthesis in the cyanobacterium Synechocystis sp. PCC 6803 is used to generate enough NADPH to drive the enzymatic reduction of cyclic ketones to their corresponding lactones. This reaction is catalyzed by the cyclohexanone monooxygenase (CHMO) from Acinetobacter calcoaceticus NCIMB 9871[1]. However, the reduction of saturated cyclic ketones by native alcoholdehydrogenases (ADHs) in Synechocysits sp. lower conversion rates. Minimized ketone concentrations and accelerated reactions toward the lactone would decrease the influence of ketoreduction. Here, the CHMO is combined with the ene-reductase YqjM of Bacillus subtilis in an cascade reaction. For now, both enzymes are expressed in different cells which were mixed for in vivo biotransformations. This offers the possibility to compensate expression levels and enzyme activities by precisely dosing both cells. However, coexpression of both enzymes would simplify the work progress and would prevent transport problems between the cells.

AB - Photosynthesis in the cyanobacterium Synechocystis sp. PCC 6803 is used to generate enough NADPH to drive the enzymatic reduction of cyclic ketones to their corresponding lactones. This reaction is catalyzed by the cyclohexanone monooxygenase (CHMO) from Acinetobacter calcoaceticus NCIMB 9871[1]. However, the reduction of saturated cyclic ketones by native alcoholdehydrogenases (ADHs) in Synechocysits sp. lower conversion rates. Minimized ketone concentrations and accelerated reactions toward the lactone would decrease the influence of ketoreduction. Here, the CHMO is combined with the ene-reductase YqjM of Bacillus subtilis in an cascade reaction. For now, both enzymes are expressed in different cells which were mixed for in vivo biotransformations. This offers the possibility to compensate expression levels and enzyme activities by precisely dosing both cells. However, coexpression of both enzymes would simplify the work progress and would prevent transport problems between the cells.

M3 - Poster

ER -