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

Citation
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
Citations number
23
Categorie Soggetti
Biology,Agriculture,"Biothechnology & Applied Migrobiology","Food Science & Tenology
ISSN journal
09168451
Volume
62
Issue
2
Year of publication
1998
Pages
407 - 411
Database
ISI
SICI code
0916-8451(1998)62:2<407:OOSCBT>2.0.ZU;2-U
Abstract
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.