of Active Pharmaceutical Ingredients (APIs). This is primarily due to the enhanced levels of selectivity and the improved sustainability of enzymatic processes on large scale, allowing the development of more efficient synthetic routes. In addition, advances in protein engineering techniques have made the optimization of enzymes for practical application a more routine process. 11 Table : Activity screen of P450 BM3 mutants against allylic ether substrates. Biotransformation conditions: 2 mM 7, P450 BM3 variant lysate, 0.5 mM NADPH, 1 mg/mL GDH, KPi pH=7.0, 15% MeOH, 100 µL scale; 30 °C, 750 rpm, 2 h. A variety of enzyme classes have been shown previously to perform stereoselective epoxidation on unactivated alkenes. We therefore proposed that through a process of initial screening followed by directed evolution, we would be able to develop an efficient enzyme capable of catalyzing our desired epoxidation reaction. Herein, we report the successful implementation of an engineered P450 BM3 variant for the asymmetric synthesis of a known chiral delamanid precursor 3a.