Self-Sufficient Baeyer-Villiger Monooxygenases: Effective Coenzyme Regeneration for Biooxygenation by Fusion Engineering

Two‐in‐one biocatalysts were engineered by the covalent fusion of NADPH‐dependent Baeyer–Villiger monooxygenases to a phosphite dehydrogenase for coenzyme regeneration (see scheme). Not only the purified fusion proteins, but also whole cells and crude cell extracts containing the enzyme conjugates,...

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Bibliographic Details
Published in:	Angewandte Chemie (International ed.) Vol. 47; no. 12; pp. 2275 - 2278
Main Authors:	Torres Pazmiño, Daniel E, Snajdrova, Radka, Baas, Bert-Jan, Ghobrial, Michael, Mihovilovic, Marko D, Fraaije, Marco W
Format:	Journal Article
Language:	English
Published:	Weinheim Wiley-VCH Verlag 07-03-2008 WILEY-VCH Verlag WILEY‐VCH Verlag
Subjects:	asymmetric catalysis Baeyer-Villiger reaction biotransformations coenzyme regeneration Coenzymes - chemistry Coenzymes - metabolism fusion enzymes Kinetics Lactones - chemistry Mixed Function Oxygenases - chemistry Mixed Function Oxygenases - metabolism Molecular Structure Protein Engineering Stereoisomerism
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Summary:	Two‐in‐one biocatalysts were engineered by the covalent fusion of NADPH‐dependent Baeyer–Villiger monooxygenases to a phosphite dehydrogenase for coenzyme regeneration (see scheme). Not only the purified fusion proteins, but also whole cells and crude cell extracts containing the enzyme conjugates, could be used to catalyze biotransformations with high efficiency. NADP+=nicotinamide adenine dinucleotide phosphate.
Bibliography:	http://dx.doi.org/10.1002/anie.200704630 ark:/67375/WNG-90VTSLF4-6 ArticleID:ANIE200704630 We thank CERC3 and the Austrian Science Fund (FWF project no. I19-B10) for funding, and W. A. van der Donk, University of Illinois, for providing the pRW2 double-mutant template. This study was conducted in association with COST action D25 - Applied Biocatalysis within the working group "Biooxidation". istex:3DB6F621985BEAC90976CFFD9BA1DA4A309822F0 Austrian Science Fund - No. I19-B10 We thank CERC3 and the Austrian Science Fund (FWF project no. I19‐B10) for funding, and W. A. van der Donk, University of Illinois, for providing the pRW2 double‐mutant template. This study was conducted in association with COST action D25 ‐ Applied Biocatalysis within the working group “Biooxidation”. ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1433-7851 1521-3773
DOI:	10.1002/anie.200704630