2015年
Modification of Chimeric (2S, 3S)-butanediol Dehydrogenase Based on Structural Information
PROTEIN AND PEPTIDE LETTERS
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- 巻
- 22
- 号
- 3
- 開始ページ
- 226
- 終了ページ
- 233
- 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
A chimeric (2S, 3S)-butanediol dehydrogenase (cLBDH) was engineered to have the strict (S)-configuration specificity of the (2S, 3S)-BDH (BsLBDH) derived from Brevibacterium saccharolyticum as well as the enzymatic stability of the (2R, 3S)-BDH (KpMBDH) from Klebsiella pneumonia by swapping the domains of two native BDHs. However, while cLBDH possesses the stability, it lacks the specificity. In order to assist in the design a BDH having strict substrate specificity, an X-ray structural analysis of a cLBDH crystal was conducted at 1.58 angstrom. The results obtained show some readily apparent differences around the active sites of cLBDH and BsLBDH. Based on this structural information, a novel (2S, 3S)-BDH having a preferred specificity was developed by introducing a V254L mutation into cLBDH. The influence of this mutation on the stability of cLBDH was not evaluated. Nevertheless, the technique described herein is an effective method for the production of a tailor-made BDH.
- リンク情報
- ID情報
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- ISSN : 0929-8665
- eISSN : 1875-5305
- Web of Science ID : WOS:000350483400004