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

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  • SATO Tsutomu
    Graduate School of Science and Technology, Niigata University
  • KANAI Yoshinori
    Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University
  • HOSHINO Tsutomu
    Graduate School of Science and Technology, Niigata University Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University

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  • Overexpression of Squalene-Hopene Cycla
  • Overexpression of Squalene-Hopene Cyclase by the pET Vector in<i>Escherichia Coli</i>and First Identification of Tryptophan and Aspartic Acid Residues inside the QW Motif as Active Sites

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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. coli BL21(DE3). Site-directed mutagenesis experiments prove that two amino acid residues of tryptophan and aspartic acid inside the QW-motif 5 resided as active sites.<br>

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