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)

Abstract

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
Volume23
Issue number5
DOIs
Publication statusPublished - 2005 Sep

Fingerprint

Escherichia coli
Amino acids
Genes
Oxidoreductases
Sinorhizobium meliloti
Amino Acids
Alanine
Plasmids
Cells
Enzymes
Growth
branched-chain-amino-acid transaminase

Keywords

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

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biotechnology
  • Catalysis

Cite this

Preparation of optically active 4-chlorophenylalanine from its racemate by deracemization technique using transformant Escherichia coli cells. / Kato, Dai Ichiro; Miyamoto, Kenji; Ohta, Hiromichi.

In: Biocatalysis and Biotransformation, Vol. 23, No. 5, 09.2005, p. 375-379.

Research output: Contribution to journalArticle

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