Enantioenriched Compounds via Enzyme-Catalyzed Redox Reactions

Major advances dealing with reductases and oxidases are summarized and organized according to important concepts in asymmetric biosynthesis. It is found that compartmentalization is necessary to avoid reversible reactions through consumption of both cofactor forms by the same enzyme. The reaction catalyzed by Old Yellow Enzyme (OYE) is stereoselective, and variability is observed throughout the whole family and has allowed the development of enzyme- and substrate-based stereocontrols. A wide range of possible substrates with bulky hydrophobic side chains are synthesized and converted by leucine dehydrogenase (LeuDH) and phenylalanine dehydrogenase (PheDH).Toluene dioxygenases (TOD) catalyze the oxidation of aromatic compounds to furnish the corresponding cis-cyclohexadiene diols and present great synthetic potential as there is currently no synthetic equivalent.