PMID:22031029
| Citation |
Seo, YM and Yun, H (2011) Enzymatic synthesis of L-tert-leucine with branched chain aminotransferase. J. Microbiol. Biotechnol. 21:1049-52 |
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| Abstract |
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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| Keywords |
Aspartate Aminotransferases/genetics; Aspartate Aminotransferases/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Glutamic Acid/metabolism; Leucine/biosynthesis; Pyruvate Decarboxylase/genetics; Pyruvate Decarboxylase/metabolism; Transaminases/genetics; Transaminases/metabolism |
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