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