Asymmetric Ene-Reduction by F420 -Dependent Oxidoreductases B (FDOR-B) from Mycobacterium smegmatis – New Paper

Industrial biocatalysts, especially for the production of pharmaceuticals and other fine chemicals, are in growing demand due to their high specificity, and lower environmental cost resulting from their inherent renewability and comparatively mild reaction conditions when compared to classical catalysts. 

The study investigated the activity of eight enzymes from a subclass of Flavin/deazaflavin oxido reductases (FDOR’s) that have previously not been researched extensively, evaluating their specific activity, kinetic properties, and stereo-selectivity against α,β-unsaturated compounds. The stereo-chemical outcomes of these enzymes was compared with results of other FDOR’s and conventional enzymes of interest. Computational modelling and induced-fit docking are used to rationalize the observed catalytic behavior and proposed a catalytic mechanism for the eight enzymes of interest. 

Although the eight enzymes of interest showed reduced catalytic activity to current industrial ene-reductases (other FDOR’s) of interest, the mechanisms explored in the paper offer insight into the reasons for this reduced catalytic behaviour, offering potential for protein engineering and optimisation of the target enzymes.

Well done to Suk Woo Kang and other researchers involved with this project. 

See the full paper here.