Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor binding
| Autor: | Philipp Rathsack, Adrie H. Westphal, Willem J. H. van Berkel, Catleen Conrad, Thomas Heine, Anika Riedel, Dirk Tischler |
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| Rok vydání: | 2015 |
| Předmět: |
Stereochemistry
functional-analysis Biophysics Biochemie Flavoprotein mechanism Biochemistry Applied Microbiology and Biotechnology Cofactor Styrene Rhodococcus opacus chemistry.chemical_compound Styrene oxide Oligomerization Monooxygenase VLAG degradation Cofactor binding FAD binding biology recombinant escherichia-coli crystal-structure Styrene epoxidation chemistry catabolism genes biology.protein Rhodococcus opacus 1CP Original Article oxide putida ca-3 pseudomonas-fluorescens st strain vlb120 |
| Zdroj: | AMB Express AMB Express 5 (2015) AMB Express, 5 |
| ISSN: | 2191-0855 |
| Popis: | Styrene monooxygenases (SMOs) are flavoenzymes catalyzing the epoxidation of styrene into styrene oxide. SMOs are composed of a monooxygenase (StyA) and a reductase (StyB). The latter delivers reduced FAD to StyA on the expense of NADH. We identified Rhodococcus opacus 1CP as the first microorganism to possess three different StyA isoforms occurring in two systems StyA1/StyA2B and StyA/StyB, respectively. The hydrodynamic properties of StyA isozymes were found to be modulated by the binding of the (reduced) FAD cofactor. StyA1 and SyA2B mainly occur as dimers in their active forms while StyA is a monomer. StyA1 showed the highest epoxidation activity and excellent enantioselectivity in aromatic sulfoxidation. The hydrodynamic and biocatalytic properties of SMOs from strain 1CP are of relevance for investigation of possible industrial applications. Electronic supplementary material The online version of this article (doi:10.1186/s13568-015-0112-9) contains supplementary material, which is available to authorized users. |
| Databáze: | OpenAIRE |
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