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Functional assembly...
Functional assembly of camphor converting two-component Baeyer-Villiger monooxygenases with a flavin reductase from E-coli
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- Kadow, Maria (author)
- Stockholms universitet,Institutionen för organisk kemi,Ernst Moritz Arndt Universitat Greifswald, Germany
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Balke, Kathleen (author)
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Willetts, Andrew (author)
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Bornscheuer, Uwe T. (author)
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- Bäckvall, Jan-Erling (author)
- Stockholms universitet,Institutionen för organisk kemi
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(creator_code:org_t)
- 2013-11-05
- 2014
- English.
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In: Applied Microbiology and Biotechnology. - : Springer-Verlag Berlin Heidelberg. - 0175-7598 .- 1432-0614. ; 98:9, s. 3975-3986
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Subject headings
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- The major limitation in the synthetic application of two-component Baeyer-Villiger monooxygenases was addressed by identifying the 28-kDa flavin-reductase Fre from Escherichia coli as a suitable supplier of reduced FMN for these enzymes. Coexpression of Fre with either 2,5- or 3,6-diketocamphane monooxygenase from Pseudomonas putida NCIMB 10007 significantly enhanced the conversion of camphor and norcamphor serving as representative ketones. With purified enzymes, full conversion was achieved, while only slight amounts of product were formed in the absence of this flavin reductase. Fusion of the genes of Fre and DKCMOs into single open reading frame constructs resulted in unstable proteins exhibiting flavin reducing, but poor oxygenating activity, which led to overall decreased conversion of camphor.
Subject headings
- NATURVETENSKAP -- Kemi -- Organisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Organic Chemistry (hsv//eng)
Keyword
- Baeyer-Villiger monooxygenases
- Multi-component flavin-dependent monooxygenases
- Pseudomonas putida NCIMB10007
- Flavin reductase
- Fre
- Fusion protein
Publication and Content Type
- ref (subject category)
- art (subject category)
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