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
T SatoT Hoshino

Abstract

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.

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Citations

May 3, 2011·Applied and Environmental Microbiology·Gabriele Siedenburg, Dieter Jendrossek
Apr 11, 2012·Proteins·Silvia RacoltaJürgen Pleiss
Mar 16, 2017·Organic & Biomolecular Chemistry·Tsutomu Hoshino
Jan 5, 2002·Bioscience, Biotechnology, and Biochemistry·T Sato, T Hoshino
Jan 15, 2009·Chemistry : a European Journal·Tsutomu HoshinoTsutomu Sato
Jan 27, 2018·Acta Crystallographica. Section F, Structural Biology Communications·Pengfei ZhouLiwen Niu
Apr 4, 2009·Organic & Biomolecular Chemistry·Jun Cheng, Tsutomu Hoshino
Oct 26, 1999·Bioorganic & Medicinal Chemistry·Y UmezawaM Nishio

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