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Functional assembly of camphor converting two-component Baeyer-Villiger monooxygenases with a flavin reductase from E-coli
Stockholm University, Faculty of Science, Department of Organic Chemistry. Ernst Moritz Arndt Universitat Greifswald, Germany.
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2014 (English)In: Applied Microbiology and Biotechnology, ISSN 0175-7598, E-ISSN 1432-0614, Vol. 98, no 9, 3975-3986 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
Springer-Verlag Berlin Heidelberg , 2014. Vol. 98, no 9, 3975-3986 p.
Keyword [en]
Baeyer-Villiger monooxygenases, Multi-component flavin-dependent monooxygenases, Pseudomonas putida NCIMB10007, Flavin reductase, Fre, Fusion protein
National Category
Organic Chemistry
Identifiers
URN: urn:nbn:se:su:diva-104410DOI: 10.1007/s00253-013-5338-3ISI: 000334433700013OAI: oai:DiVA.org:su-104410DiVA: diva2:725853
Funder
EU, European Research CouncilSwedish Research Council
Note

AuthorCount:5;

Available from: 2014-06-17 Created: 2014-06-10 Last updated: 2017-12-05Bibliographically approved

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