What is it about?
Styrene monooxygenases (SMOs) are two-enzyme systems that catalyze the enantioselective epoxidation of styrene to (S)-styrene oxide. The FADH2 co-substrate of the epoxidase component (StyA) is supplied by an NADH-dependent flavin reductase (StyB). The genome of Rhodococcus opacus 1CP encodes two SMO systems, which we define as E1 and E2-type. We found that E1-type RoStyB is inhibited by FMN, while E2-type RoStyA2B is known to be active with FMN. Optimisation of the N-terminus of RoStyB through protein engineering allowed the evolution of the activity and specificity of this reductase.
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Why is it important?
Development of styrene mono-oxygenases biocatalytic systems is of importance for a greener economy.
Perspectives
More efficient regeneration systems will boost the application of styrene mono-oxygenases.
Professor Willem J.H. van Berkel
Wageningen University
Read the Original
This page is a summary of: N -terminus determines activity and specificity of styrene monooxygenase reductases, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, September 2017, Elsevier,
DOI: 10.1016/j.bbapap.2017.09.004.
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