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KMID : 0545120110210101049
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Journal of Microbiology and Biotechnology
2011 Volume.21 No. 10 p.1049 ~ p.1052
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Enzymatic Synthesis of L-tert-Leucine with Branched Chain Aminotransferase
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Seo Young-Man
Yun Hyung-Don
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Abstract
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In this study, we demonstrated the asymmetric synthesis of L-tert-leucine from trimethylpyruvate using branchedchain 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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KEYWORD
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aminotransferase, branched chain aminotransferase, coupling reaction, L-tert-leucine, unnatural amino acid
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