A Chimeric Styrene Monooxygenase with Increased Efficiency in Asymmetric Biocatalytic Epoxidation.

ABSTRACT: The styrene monooxygenase (SMO) system from Pseudomonas sp. consists of two enzymes (StyA and StyB). StyB catalyses the reduction of FAD at the expense of NADH. After the transfer of FADH₂ from StyB to StyA, reaction with O₂ generates FAD-OOH, which is the epoxidising agent. The wastage of redox equivalents due to partial diffusive transfer of FADH₂ , the insolubility of recombinant StyB and the impossibility of expressing StyA and StyB in a 1:1 molar ratio reduce the catalytic efficiency of the natural system. Herein we present a chimeric SMO (Fus-SMO) that was obtained by genetic fusion of StyA and StyB through a flexible linker. Thanks to a combination of: 1) balanced and improved expression levels of reductase and epoxidase units, and 2) intrinsically h

SUBMITTER: Corrado ML 

PROVIDER: S-EPMC5900736 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature