Journal of Bioscience and Bioengineering 2007-11-01

Purification and characterization of 2-aminoacetophenone reductase of newly isolated Burkholderia sp. YT.

Keiko Yamada-Onodera, Yuhki Takase, Yoshiki Tani

Index: J. Biosci. Bioeng. 104(5) , 416-9, (2007)

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Abstract

We found that a newly isolated Burkholderia sp. produced (R)-2-amino-1-phenylethanol from 2-aminoacetophenone, showing the high stereospecificity. NADPH-dependent 2-aminoacetophenone reductase purified to homogeneity was a dimer with a molecular mass of 65,000. The purified enzyme did not reduce acetophenone and 1-phenyl-1-propanone. The purified enzyme converted 2-aminoacetophenone to only (R)-2-amino-1-phenylethanol.