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Asymmetric synthesis using transaminase and expanding its substrate spectra

초록

영어

Asymmetric synthesis using efficient chemical or biocatalyst is the most desirable approach to synthesize chiral compounds. Transaminase can be used for the purpose of the production of chiral amino acids and amines. In general, alpha-transaminase has very low equilibrium constant, so that asymmetric synthesis is relatively easy to be developed, whereas w-transaminase has rather high equilibrium constant, so that more rigorous limitations always exist for the similar asymmetric synthesis. To understand these limitations in depth, we have mechanistically studied the half reaction of the transamination reaction. To design better asymmetric synthesis process, variations of amine group donor substrates were attempted, and underlying criteria to select a proper partner(amine donor) were analyzed, and the results will be discussed. In addition, to exploit better and broad applications of transaminase for the synthesis of chiral amine compounds, few examples of newly screened w-transaminases for target products, especially the compounds with double chiral centers, will be discussed, and computational strategies for expanding the substrate spectra of such transaminases were further attempted using homology modeling and sequence analysis. Their evaluation results will be presented.

저자정보

  • Byung-Gee Kim Division of Chemical and Biological Engineering, Seoul National Univesrity
  • Ju-Hyun Seo Division of Chemical and Biological Engineering, Seoul National Univesrity,
  • Min-Ho Cha Division of Chemical and Biological Engineering, Seoul National Univesrity,
  • Do-Hyun Kyung Division of Chemical and Biological Engineering, Seoul National Univesrity,
  • Jun-Hyung Hwang Division of Chemical and Biological Engineering, Seoul National Univesrity,
  • Hyung-Youn Park Division of Chemical and Biological Engineering, Seoul National Univesrity,

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