DOI QR코드

DOI QR Code

Enzymatic Synthesis of L-tert-Leucine with Branched Chain Aminotransferase

  • 투고 : 2011.05.25
  • 심사 : 2011.06.19
  • 발행 : 2011.10.28

초록

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.

키워드

참고문헌

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