期刊
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
卷 21, 期 10, 页码 1049-1052出版社
KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
DOI: 10.4014/jmb.1105.05049
关键词
Aminotransferase; branched-chain aminotransferase; coupling reaction; L-tert-leucine; unnatural amino acid
资金
- Yeungnam University [209-A-380-055]
In this study, we demonstrated the asymmetric synthesis of L-tert-leucine from trimethylpyruvate using branched-chain aminotransferase (BCAT) from Escherichia coli in the presence of L-glutamate as an amino donor. Since BCAT was severely inhibited by 2-ketoglutarate, in order to overcome this here, we developed a BCAT/aspartate aminotransferase (AspAT) and BCAT/AspAT/pyruvate decarboxylase (PDC) coupling reaction. In the BCAT/AspAT/PDC coupling reaction, 89.2 mM L-tert-leucine (ee >99%) was asymmetrically synthesized from 100 mM trimethylpyruvate.
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