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.
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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pET 载体在大肠杆菌中过度表达角鲨烯-霍烯环化酶，并首次鉴定出 QW 基序内的色氨酸和天冬氨酸残基作为活性位点。
DOI：
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发表时间：
1998
期刊：
影响因子：
--
通讯作者：
T. Hoshino
中科院分区：
文献类型：
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作者：
T. Sato;Y. Kanai;T. Hoshino
构建了角鲨烯-霍烯环化酶（SHC）的高效表达载体pET 3a，该载体在T7强启动子的作用下能高效表达SHC。coli BL21（DE3）。定点突变实验证明，QW基序5内的色氨酸和天冬氨酸两个氨基酸残基是活性位点。
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.
DOI：
10.1073/pnas.92.20.9274
发表时间：
1995-09-26
影响因子：
11.1
作者：
ABE, I;PRESTWICH, GD
通讯作者：
PRESTWICH, GD