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
T. Sato et al., 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, Bioscience, biotechnology, and biochemistry, 62(2), 1998, pp. 407-411
An overexpression system for squalene-hopene cyclase (SHC) was constru
cted by using the pET3a vector, which is responsible for high expressi
on with help from the strong T7 promoter when incorporated into E. col
i BL21(DE3). Site-directed mutagenesis experiments prove that two amin
o acid residues of tryptophan and aspartic acid inside the QW-motif 5
resided as active sites.