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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Purification and characterization of 2-aminoacetophenone reductase of newly isolated Burkholderia sp. YT. Yamada-Onodera, K., Takase, Y., Tani, Y. J. Biosci. Bioeng. (2007) [Pubmed]
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