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)
Full Text: HTML
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.
Related Compounds
Related Articles:
Quantitative analysis of 2-aminoacetophenone in off-flavored wines by stable isotope dilution assay.
1996-01-01
[J. AOAC Int. 79(2) , 583-6, (1996)]
2009-12-01
[J. Pharm. Sci. 98(12) , 4639-49, (2009)]
Effectiveness of thirteen vertebrate repellents as rodent trigeminal stimulants.
1996-12-01
[Physiol. Behav. 60(6) , 1449-52, (1996)]
Maternal ingestion of ortho-aminoacetophenone during gestation affects intake by offspring.
1995-11-01
[Physiol. Behav. 58(5) , 925-8, (1995)]
Transformation of 2-aminoacetophenone to ( S) -2-amino-1-phenylethanol by Arthrobacter sulfureus.
2004-08-01
[Biotechnol. Lett. 26(16) , 1255-9, (2004)]