Construction of a tailor-made L (2S,3S)-butanediol dehydrogenase by exchanging domains between native structural analogs |
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Authors: | Shimegi Tomohito Takusagawa Yuhsuke Ohtsuki Takashi Noda Satoko Kurisu Genji Kusunoki Masami Ui Sadaharu |
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Institution: | Graduate School of Medicine and Engineering, University of Yamanashi, Takeda, Kofu, Japan. |
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Abstract: | The development of a stable L-BDH chimera was attempted by exchanging whole domains between two native structural analogs, L-BDH and meso-BDH, because the S-configuration specificity of L-BDH is valuable from the standpoint of its application but its activity is unstable, whereas meso-BDH is stable. The domain chimeras obtained indicated that the leaf-like structures constituting three domains were likely to be mainly associated with chiral recognition, and the fourth domain, the basic domain, is likely to be mainly associated with enzyme stability. A combination of the leaf domains of L-BDH and the basic domain of meso-BDH attained a sufficient level of practical use as an artificial L-BDH chimera, because the resulting enzyme had both stability and S-configuration specificity. However, the levels of stability and specificity were slightly lower than those of the respective enzymes from which they were derived. |
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