Purification and characterization of a novel NADPH-dependent 2-aminoacetophenone reductase from Arthrobacter sulfureus

Abstract

A novel 2-aminoacetophenone reductase was purified to homogeneity from Arthrobacter sulfureus BW1010. The enzyme is a monomer with a molecular weight of approximately 60kDa. Using NADPH as coenzyme, it catalyzes the reduction of ketones, especially amine phenyl ketones, and stereospecifically reduces 2-aminoacetophenone to (S)-2-amino-1-phenylethanol (e.e>99.8%) with the optimal pH at 7.5.