Preparation of optically active 4-chlorophenylalanine from its racemate by deracemization technique using transformant Escherichia coli cells

Dai Ichiro Kato, Kenji Miyamoto, Hiromichi Ohta

Research output: Contribution to journalArticle

13 Citations (Scopus)


We have developed a method for the preparation of L-4-chlorophenylalanine from its racemate with Escherichia coli cells expressing a single foreign gene. L-4-Chlorophenylalanine was obtained in a high optical yield by the inversion of configuration of its d-form via the tandem reactions catalyzed by d-amino acid dehydrogenase (DadA) and branched-chain amino acid aminotransferase (BCAAT). While we constructed a plasmid for BCAAT utilizing the gene from Sinorhizobium meliloti ATCC 51124, the first enzyme DadA was the dadA-gene product from E. coli host cell itself, which was activated by the addition of L-alanine in the growth medium.

Original languageEnglish
Pages (from-to)375-379
Number of pages5
JournalBiocatalysis and Biotransformation
Issue number5
Publication statusPublished - 2005 Sep 1



  • Branched-chain amino acid aminotransferase gene
  • DadA gene activation
  • Microbial deracemization
  • Preparation of L-4-chlorophenylalanine

ASJC Scopus subject areas

  • Biotechnology
  • Catalysis
  • Biochemistry

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