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

Article abstract of DOI:10.1271/bbb.62.407

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.