Overexpression of Squalene-Hopene Cyclase by the pET Vector in Escherichia Coil and First Identification of Tryptophan and Aspartic Acid Residues inside the QW Motif as Active Sites

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概要

• 論文の詳細を見る

• An overexpression system for squalene-hopene cyclase(SHC) was constructed by using the pET3a vector, which is responsible for high expression with help from the strong T7 promoter when incorporated into E.coil BL21(DE3).Site-directed mutabenesis experiments prove that two amino acid residues of tryptophan and aspartic acid inside the QW-motif 5 resided as active sites.

• 社団法人日本農芸化学会の論文
• 1998-02-23

著者

• Kanai Y

  Department Of Applied Biolobical Chemistry Faculty Of Agriculture Niigata University

• Kanai Yoshinori

  Department Of Internal Medicine And Rheumatology Juntendo University School Of Medicine

• Sato T

  Iwate Biotechnology Research Center:department Of Biotechnology And Environmental Chemistry National

• SATO TSUTOMU

  Graduate School of Engineering, Hokkaido University

• Hoshino Tsutomu

  Department Of Applied Biological Chemistry Faculty Of Agriculture And Graduate School Of Science And

• Hoshino Tsutomu

  Graduate School Of Science And Technology Faculty Of Agriculture Niigata University:(present Address

• Hoshino Tsutomu

  Department Of Applied Biological Chemistry Faculty Of Agriculture And Graduate School Of Science And

• Hoshino Tsutomu

  Graduate School Of Science And Technology And Department Of Applied Biolobical Chemistry Faculty Of

• Hoshino Tsutomu

  Graduate School Of Engineering Kyoto University

• Sato Tsutomu

  Graduate School Of Engineering Hokkaido University

• Sato Tsutomu

  Graduate School Of Science And Technology Faculty Of Agriculture Niigata University

• Sato Tsutomu

  Graduate School Of Science And Technology

• Kanai Yoshinori

  Department of Applied Biolobical Chemistry, Faculty of Agriculture, Niigata University

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