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.
Yamada-Onodera
Keiko
K
Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma 630-0192, Japan. onoderak@bs.naist.jp <onoderak@bs.naist.jp>
Takase
Yuhki
Y
Tani
Yoshiki
Y
D000098:Acetophenones / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D001592:Benzyl Alcohols / Q000737:chemistry / Q000378:metabolism*; D019117:Burkholderia / Q000201:enzymology*; D019281:Dimerization; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification; D013379:Substrate Specificity
D000098:Acetophenones; D001592:Benzyl Alcohols; C523155:2-amino-1-phenylethanol; C055495:2-aminoacetophenone; C007656:alpha-ethylbenzyl alcohol; D010088:Oxidoreductases; C038699:acetophenone