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Mutagenesis-Independent Stabilization of Class B Flavin Monooxygenases in Operation.
- Source :
-
Advanced Synthesis & Catalysis . Jun2017, Vol. 359 Issue 12, p2121-2131. 11p. - Publication Year :
- 2017
-
Abstract
- This paper describes the stabilization of flavin-dependent monooxygenases under reaction conditions, using an engineered formulation of additives (the natural cofactors NADPH and FAD, and superoxide dismutase and catalase as catalytic antioxidants). This way, a 103- to 104-fold increase of the half-life was reached without resource-intensive directed evolution or structure-dependent protein engineering methods. The stabilized enzymes are highly valued for their synthetic potential in biotechnology and medicinal chemistry (enantioselective sulfur, nitrogen and Baeyer-Villiger oxidations; oxidative human metabolism), but widespread application was so far hindered by their notorious fragility. Our technology immediately enables their use, does not require structural knowledge of the biocatalyst, and creates a strong basis for the targeted development of improved variants by mutagenesis. [ABSTRACT FROM AUTHOR]
- Subjects :
- *FLAVINS
*MUTAGENESIS
*MONOOXYGENASES
*PHARMACEUTICAL chemistry
*BIOTECHNOLOGY
Subjects
Details
- Language :
- English
- ISSN :
- 16154150
- Volume :
- 359
- Issue :
- 12
- Database :
- Academic Search Index
- Journal :
- Advanced Synthesis & Catalysis
- Publication Type :
- Academic Journal
- Accession number :
- 123671450
- Full Text :
- https://doi.org/10.1002/adsc.201700585