N -terminus determines activity and specificity of styrene monooxygenase reductases

Thomas Heine, Anika Scholtissek, Adrie H. Westphal, Willem J.H. van Berkel, Dirk Tischler
  • Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, September 2017, Elsevier
  • DOI: 10.1016/j.bbapap.2017.09.004

N -terminus determines activity and specificity of styrene monooxygenase reductase

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.

Why is it important?

Development of styrene mono-oxygenases biocatalytic systems is of importance for a greener economy.


Professor Willem J.H. van Berkel
Wageningen University

More efficient regeneration systems will boost the application of styrene mono-oxygenases.

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The following have contributed to this page: Dr Dirk Tischler and Professor Willem J.H. van Berkel