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Enantioselective N-acetylation of 2-phenylglycine by an unusual N-acetyltransferase from Chryseobacterium sp.

Authors
  • Takenaka, Shinji1
  • Honma, Yuuta1
  • Yoshida, Kenji1
  • Yoshida, Ken-ichi1
  • 1 Graduate School of Agricultural Science, Kobe University, Department of Agrobioscience, 1-1 Rokkodai Nada-ku, Kobe, 657-8501, Japan , Kobe (Japan)
Type
Published Article
Journal
Biotechnology Letters
Publisher
Springer-Verlag
Publication Date
Mar 12, 2013
Volume
35
Issue
7
Pages
1053–1059
Identifiers
DOI: 10.1007/s10529-013-1172-z
Source
Springer Nature
Keywords
License
Yellow

Abstract

The demand for d-2-phenylglycine used to synthesize semisynthetic antibiotics and pesticides is increasing. We have isolated a Chryseobacterium sp. that selectively transformed the l-form of racemic d,l-2-phenylglycine to (2S)-2-acetylamide-2-phenylacetic acid with a molar yield of 50 % and an enantiomer excess of >99.5 % under optimal culture conditions, consequently resulting in 99 % pure d-2-phenylglycine remaining in the culture. The enantioselective N-acetylation was catalyzed by an acetyl-CoA-dependent N-acetyltransferase whose synthesis was induced by l-2-phenylglycine. The enzyme differed from previously reported bacterial arylamine N-acetyltransferases in molecular mass and substrate specificity. The relative activity ratio of the enzyme with the substrates l-2-phenylglycine, d-2-phenylglycine, 2-(2-chlorophenyl)glycine, and 5-aminosalicylic acid (a good substrate of arylamine N-acetyltransferase) was 100:0:56.9:5.49, respectively. The biotransformation by the N-acetyltransferase-producing bacterium reported here could constitute a new preparative route for the enzymatic resolution of d,l-2-phenylglycine.

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