Purification and characterization of a novel NADPH-dependent 2-aminoacetophenone reductase from Arthrobacter
Guogang Zhao1, Wanru Sun2, Jianjun Wang2
1State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, PR China; Department of Internal Medicine, University of Kentucky School of Medicine, Lexington, KY 40536, USA.
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 60 kDa. 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.
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