2011年8月
Construction of a Tailor-Made L (2S, 3S)-Butanediol Dehydrogenase by Exchanging Domains Between Native Structural Analogs
PROTEIN AND PEPTIDE LETTERS
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- 巻
- 18
- 号
- 8
- 開始ページ
- 825
- 終了ページ
- 830
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- 出版者・発行元
- BENTHAM SCIENCE PUBL LTD
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.
- リンク情報
- ID情報
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- ISSN : 0929-8665
- Web of Science ID : WOS:000293852700009