Enantioselective N-Acetylation of 3-Amino-3-phenylpropionic Acid by Cell-free Extracts of Streptomyces neyagawaensis

  • Chung, Myung-Chul (Enzyme Inhibition Research Unit, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Lee, Ho-Jae (Enzyme Inhibition Research Unit, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Lee, Choong-Hwan (Enzyme Inhibition Research Unit, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Chun, Hyo-Kon (Enzyme Inhibition Research Unit, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Kho, Yung-Hee (Enzyme Inhibition Research Unit, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
  • Published : 1997.10.01

Abstract

Cell-free extracts of Streptomyces neyagawaensis SL-387 grown on a chemically defined medium supplemented with DL-3-amino-3-phenylpropionic acid (APP) produced N-acetyl-APP (Ac-APP) in the presence of APP and acetyl coenzyme A. The APP obtained by acid hydrolysis of the Ac-APP was D-configuration: $[\alpha]_D+6.5^{\circ}(H_2O)\;at\;20^{\circ}C$, optical purity 92% enantiomeric excesses (ee). These results suggest that an N-acetyltransferase exists in the cell-free extract as a novel enzyme with specificity for D-APP.

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