Identification, Cloning, and Characterization of a Novel Ketoreductase from the Cyanobacterium
            <i>Synechococcus</i>
            sp. Strain PCC 7942

Hölsch, Kathrin; Havel, Jan; Haslbeck, Martin; Weuster‐Botz, Dirk

doi:10.1128/aem.00925-08

Cited by 36 publications

(33 citation statements)

References 30 publications

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“…PCC 7942, which is involved in the reduction of multi-halogenated and sterically demanding ketones (4-chloroacetoacetate; 2′,3′,4′,5′,6′-pentafluoroacetophenone) with excellent enantioselectivity (>99.8%, S), has been identified as 3-ketoacyl-(acyl-carrier-protein) reductase (EC 1.1.1.100) and this is effective inside the cells under an optimal light regime. 23 Homologous reductases have also been found in other cyanobacterial strains belonging to different taxonomic groups (Nostocales, Oscillatoriales, Chroococcales). 24 These are defined as crucial for the metabolism of many endogenous and xenobiotic compounds, given their variable specificities and activities.…”

Section: Resultsmentioning

confidence: 99%

Application of cyanobacteria for chiral phosphonate synthesis

Górak

Żymańczyk–Duda

2015

Green Chem.

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This is the first report on morphologically different strains of cyanobacteria: Arthrospira maxima, Nostoc cf-muscorum and Nodularia sphaerocarpa used for enantioselective bioreduction of selected, structurally different diethyl esters of oxophosphonic acids. The efficiency of the asymmetric hydrogen transfer was strongly dependent on the chemical structure of the substrates. Arthrospira maxima was active only toward diethyl (S)-2-oxopropylphosphonate (20% of yield, 99% of ee), whereas the application of Nostoc cf-muscorum as a biocatalyst allowed diethyl (S)-2-hydroxy-2-phenylethylphosphonate with a high enantiomeric excess (99%) and with 26% conversion degree to be obtained. Employing Nodularia sphaerocarpa led to the most spectacular result -diethyl (S)-2-hydroxy-2-phenylethylphosphonate with a degree of conversion of 99% and an optical purity of 92%. Enantioselective bioconversion of oxophosphonate with an aromatic side group located in the immediate vicinity of the carbonyl functionality was achieved for the first time. Additionally, flow cytometry showed excellent resistance of the cells of Nodularia sphaerocarpa against the examined xenobiotic -2-oxo-2-phenylethylphosphonate, these cells remain viable at the concentration of 10 mM of the bioconversion substrate compared to the 1 mM described previously for a fungal biocatalyst. The effect of cultivation medium, light source and light cycle (light : dark) on the effectiveness of the biotransformation process was examined.

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Section: Resultsmentioning

confidence: 99%

Application of cyanobacteria for chiral phosphonate synthesis

Górak

Żymańczyk–Duda

2015

Green Chem.

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“…Table 3 Enantioselective reduction of aryl ketones, a-and b-ketoesters by ScCR. (Hölsch et al, 2008). In those cases, the presence of the ester group determines which product is formed and the steric aspect is less important (Hölsch and Weuster-Botz, 2010).…”

Section: Substrate Specificity and Enantioselectivitymentioning

confidence: 97%

Highly efficient synthesis of chiral alcohols with a novel NADH-dependent reductase from Streptomyces coelicolor

Wang¹,

Li²,

Ni³

et al. 2011

Bioresource Technology

135

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“…Hölsch et al demonstrated that an alcohol dehydrogenase from Synechococcus sp. strain PCC7942 [16] shows a strong preference for NADPH. Therefore, exposure of the cells to high-intensity light supplies redox equivalents for heterologous enzymes on the one hand, but on the other hand also provides optimal conditions for alternative redox reactions, catalysed by host enzymes.…”

Section: Discussionmentioning

confidence: 99%

Enzymatic Oxyfunctionalization Driven by Photosynthetic Water-Splitting in the Cyanobacterium Synechocystis sp. PCC 6803

et al. 2017

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Photosynthetic water-splitting is a powerful force to drive selective redox reactions. The need of highly expensive redox partners such as NADPH and their regeneration is one of the main bottlenecks for the application of biocatalysis at an industrial scale. Recently, the possibility of using the photosystem of cyanobacteria to supply high amounts of reduced nicotinamide to a recombinant enoate reductase opened a new strategy for overcoming this hurdle. This paper presents the expansion of the photosynthetic regeneration system to a Baeyer-Villiger monooxygenase. Despite the potential of this strategy, this work also presents some of the encountered challenges as well as possible solutions, which will require further investigation. The successful enzymatic oxygenation shows that cyanobacterial whole-cell biocatalysis is an applicable approach that allows fuelling selective oxyfunctionalisation reactions at the expense of light and water. Yet, several hurdles such as side-reactions and the cell-density limitation, probably due to self-shading of the cells, will have to be overcome on the way to synthetic applications.

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Identification, Cloning, and Characterization of a Novel Ketoreductase from the Cyanobacterium Synechococcus sp. Strain PCC 7942

Cited by 36 publications

References 30 publications

Application of cyanobacteria for chiral phosphonate synthesis

Application of cyanobacteria for chiral phosphonate synthesis

Highly efficient synthesis of chiral alcohols with a novel NADH-dependent reductase from Streptomyces coelicolor

Enzymatic Oxyfunctionalization Driven by Photosynthetic Water-Splitting in the Cyanobacterium Synechocystis sp. PCC 6803

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