期刊
BIOCATALYSIS AND BIOTRANSFORMATION
卷 23, 期 5, 页码 375-379出版社
TAYLOR & FRANCIS LTD
DOI: 10.1080/10242420500296295
关键词
branched-chain amino acid aminotransferase gene; preparation of L-4-chlorophenylalanine; microbial deracemization; dadA gene activation
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.
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